Skip to main content
Bacteriological Reviews logoLink to Bacteriological Reviews
. 1970 Sep;34(3):278–343. doi: 10.1128/br.34.3.278-343.1970

Pyrimidine metabolism in microorganisms.

G A O'Donovan, J Neuhard
PMCID: PMC378357  PMID: 4919542

Full text

PDF
278

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ABRAMS R., DURAISWAMI S. DEOXYCYTIDYLATE FORMATION FROM CYTIDYLATE WITHOUT GLYCOSIDIC CLEAVAGE IN LACTOBACILLUS LEICHMANNII EXTRACTS CONTAINING VITAMIN B12 COENZYME. Biochem Biophys Res Commun. 1965 Feb 3;18:409–414. doi: 10.1016/0006-291x(65)90722-9. [DOI] [PubMed] [Google Scholar]
  2. AMES B. N., GARRY B., HERZENBERG L. A. The genetic control of the enzymes of histidine biosynthesis in Salmonella typhimurium. J Gen Microbiol. 1960 Apr;22:369–378. doi: 10.1099/00221287-22-2-369. [DOI] [PubMed] [Google Scholar]
  3. ANDERSON E. P., BROCKMAN R. W. FEEDBACK INHIBITION OF URIDINE KINASE BY CYTIDINE TRIPHOSPHATE AND URIDINE TRIPHOSPHATE. Biochim Biophys Acta. 1964 Nov 15;91:380–386. doi: 10.1016/0926-6550(64)90067-2. [DOI] [PubMed] [Google Scholar]
  4. ANDERSON E. P., LAW L. W. Biochemistry of cancer. Annu Rev Biochem. 1960;29:577–608. doi: 10.1146/annurev.bi.29.070160.003045. [DOI] [PubMed] [Google Scholar]
  5. Abbott M. T., Dragila T. A., McCroskey R. P. The formation of 5-formyluracil by cell-free preparations from Neurospora crassa. Biochim Biophys Acta. 1968 Nov 20;169(1):1–6. doi: 10.1016/0005-2787(68)90002-6. [DOI] [PubMed] [Google Scholar]
  6. Abbott M. T., Schandl E. K., Lee R. F., Parker T. S., Midgett R. J. Cofactor requirements of thymine 7-hydroxylase. Biochim Biophys Acta. 1967 Mar 15;132(2):525–528. doi: 10.1016/0005-2744(67)90177-5. [DOI] [PubMed] [Google Scholar]
  7. Abd-el-Al A. Arginine-auxotrophic phenotype resulting from a mutation in the pryA gene of Escherichia coli B-r. J Bacteriol. 1969 Jan;97(1):466–468. doi: 10.1128/jb.97.1.466-468.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Abd-el-Al A., Ingraham J. L. Cold sensitivity and other phenotypes resulting from mutation in pyrA gene. J Biol Chem. 1969 Aug 10;244(15):4039–4045. [PubMed] [Google Scholar]
  9. Abd-el-Al A., Ingraham J. L. Control of carbamyl phosphate synthesis in Salmonella typhimurium. J Biol Chem. 1969 Aug 10;244(15):4033–4038. [PubMed] [Google Scholar]
  10. Abeles R. H., Beck W. S. The mechanism of action of cobamide coenzyme in the ribonucleotide reductase reaction. J Biol Chem. 1967 Aug 25;242(16):3589–3593. [PubMed] [Google Scholar]
  11. Abrams R. Cytidine 5'-triphosphate as the precursor of deoxycytidylate in Lactobacillus leichmannii. J Biol Chem. 1965 Sep;240(9):3697–3697. [PubMed] [Google Scholar]
  12. Ahmad S. I., Barth P. T., Pritchard R. H. Properties of a mutant of Escherichia coli lacking purine nucleoside phosphorylase. Biochim Biophys Acta. 1968 Jul 23;161(2):581–583. doi: 10.1016/0005-2787(68)90140-8. [DOI] [PubMed] [Google Scholar]
  13. Ahmad S. I., Pritchard R. H. A map of four genes specifying enzymes involved in catabolism of nucleosides and deoxynucleosides in Escherichia coli. Mol Gen Genet. 1969 Aug 15;104(4):351–359. doi: 10.1007/BF00334234. [DOI] [PubMed] [Google Scholar]
  14. Albrecht A. M., Pearce F. K., Hutchison D. J. Folate coenzymes in amethopterin-sensitive and -resistant strains of Streptococcus faecalis. Enzymatic formation and metabolic function. J Biol Chem. 1966 Mar 10;241(5):1036–1042. [PubMed] [Google Scholar]
  15. Aleman V., Handler P. Dihydroorotate dehydrogenase. I. General properties. J Biol Chem. 1967 Sep 25;242(18):4087–4096. [PubMed] [Google Scholar]
  16. Alikhanian S. I., Iljina T. S., Kaliaeva E. S., Kameneva S. V., Sukhodolec V. V. A genetical study of thymineless mutants of E. coli K12. Genet Res. 1966 Aug;8(1):83–100. doi: 10.1017/s0016672300009939. [DOI] [PubMed] [Google Scholar]
  17. Ames B. N., Garry B. COORDINATE REPRESSION OF THE SYNTHESIS OF FOUR HISTIDINE BIOSYNTHETIC ENZYMES BY HISTIDINE. Proc Natl Acad Sci U S A. 1959 Oct;45(10):1453–1461. doi: 10.1073/pnas.45.10.1453. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Anderson P. M., Marvin S. V. Effect of allosteric effectors and adenosine triphosphate on the aggregation and rate of inhibition by N-ethylmaleimide of carbamyl phosphate synthetase of Escherichia coli. Biochemistry. 1970 Jan 6;9(1):171–178. doi: 10.1021/bi00803a022. [DOI] [PubMed] [Google Scholar]
  19. Anderson P. M., Marvin S. V. Effect of ornithine, IMP, and UMP on carbamyl phosphate synthetase from Escherichia coli. Biochem Biophys Res Commun. 1968 Sep 30;32(6):928–934. doi: 10.1016/0006-291x(68)90116-2. [DOI] [PubMed] [Google Scholar]
  20. Anderson P. M., Meister A. Control of Escherichia coli carbamyl phosphate synthetase by purine and pyrimidine nucleotides. Biochemistry. 1966 Oct;5(10):3164–3169. doi: 10.1021/bi00874a013. [DOI] [PubMed] [Google Scholar]
  21. Anderson P. M., Meister A. Evidence for an activated form of carbon dioxide in the reaction catalyzed by Escherichia coli carbamyl phosphate synthetase. Biochemistry. 1965 Dec;4(12):2803–2809. doi: 10.1021/bi00888a034. [DOI] [PubMed] [Google Scholar]
  22. Appel S. H. Purification and kinetic properties of brain orotidine 5'-phosphate decarboxylase. J Biol Chem. 1968 Jul 25;243(14):3924–3929. [PubMed] [Google Scholar]
  23. BAGATELL F. K., WRIGHT E. M., SABLE H. Z. Biosynthesis of ribose and deoxyribose in Escherichia coli. J Biol Chem. 1959 Jun;234(6):1369–1374. [PubMed] [Google Scholar]
  24. BARNER H. D., COHEN S. S. The induction of thymine synthesis by T2 infection of a thymine requiring mutant of Escherichia coli. J Bacteriol. 1954 Jul;68(1):80–88. doi: 10.1128/jb.68.1.80-88.1954. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. BARNER H. D., COHEN S. S. Virus-induced acquisition of metabolic function. IV. Thymidylate synthetase in thymine-requiring Escherichia coli infected by T2 and T5 bacteriophages. J Biol Chem. 1959 Nov;234:2987–2991. [PubMed] [Google Scholar]
  26. BECK W. S., LEVIN M. Purification, kinetics, and repression control of bacterial trans-N-deoxyribosylase. J Biol Chem. 1963 Feb;238:702–709. [PubMed] [Google Scholar]
  27. BECKWITH J. R., PARDEE A. B., AUSTRIAN R., JACOB F. Coordination of the synthesis of the enzymes in the pyrimidine pathway of E. coli. J Mol Biol. 1962 Dec;5:618–634. doi: 10.1016/s0022-2836(62)80090-4. [DOI] [PubMed] [Google Scholar]
  28. BERG P., JOKLIK W. K. Enzymatic phosphorylation of nucleoside diphosphates. J Biol Chem. 1954 Oct;210(2):657–672. [PubMed] [Google Scholar]
  29. BERG P., JOKLIK W. K. Transphosphorylation between nucleoside polyphosphates. Nature. 1953 Nov 28;172(4387):1008–1009. doi: 10.1038/1721008a0. [DOI] [PubMed] [Google Scholar]
  30. BERTANI L. E., HAEGGMARK A., REICHARD P. ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES. II. FORMATION AND INTERCONVERSION OF DEOXYURIDINE PHOSPHATES. J Biol Chem. 1963 Oct;238:3407–3413. [PubMed] [Google Scholar]
  31. BLAKLEY R. L. COBAMIDES AND RIBONUCLEOTIDE REDUCTION. I. COBAMIDE STIMULATION OF RIBONUCLEOTIDE REDUCTION IN EXTRACTS OF LACTOBACILLUS LEICHMANNII. J Biol Chem. 1965 May;240:2173–2180. [PubMed] [Google Scholar]
  32. BLAKLEY R. L., McDOUGALL B. M. The biosynthesis of thymidylic acid. III. Purification of thymidylate synthetase and its spectrophotometric assay. J Biol Chem. 1962 Mar;237:812–818. [PubMed] [Google Scholar]
  33. BLAKLEY R. L., RAMASASTRI B. V., MCDOUGALL B. M. THE BIOSYNTHESIS OF THYMIDYLIC ACID. V. HYDROGEN ISOTOPE STUDIES WITH DIHYDROFOLIC REDUCTASE AND THYMIDYLATE SYNTHETASE. J Biol Chem. 1963 Sep;238:3075–3079. [PubMed] [Google Scholar]
  34. BOLTON E. T., REYNARD A. M. Utilization of purine and pyrimidine compounds in nucleic acid synthesis by Escherichia coli. Biochim Biophys Acta. 1954 Mar;13(3):381–385. doi: 10.1016/0006-3002(54)90345-5. [DOI] [PubMed] [Google Scholar]
  35. BRENNER S., SMITH J. D. Induction of mutations in the deoxyribonucleic acid of phage T2 synthesized in the presence of chloramphenicol. Virology. 1959 May;8(1):124–125. doi: 10.1016/0042-6822(59)90024-8. [DOI] [PubMed] [Google Scholar]
  36. BRESNICK E., SINGER S., HITCHINGS G. H. Mechanism of action of 6-azacytosine in bacteria. Biochim Biophys Acta. 1960 Jan 15;37:251–257. doi: 10.1016/0006-3002(60)90231-6. [DOI] [PubMed] [Google Scholar]
  37. BROCKMAN R. W., DAVIS J. M., STUTTS P. Metabolism of uracil and 5-fluorouracil by drug-sensitive and by drug-resistant bacteria. Biochim Biophys Acta. 1960 May 6;40:22–32. doi: 10.1016/0006-3002(60)91311-1. [DOI] [PubMed] [Google Scholar]
  38. BROOKE M. S., USHIBA D., MAGASANIK B. Some factors affecting the excretion of orotic acid by mutants of Aerobacter aerogenes. J Bacteriol. 1954 Nov;68(5):534–540. doi: 10.1128/jb.68.5.534-540.1954. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Barth P. T., Beacham I. R., Ahmad S. I., Pritchard R. H. The inducer of the deoxynucleoside phosphorylases and deoxyriboaldolase in Escherichia coli. Biochim Biophys Acta. 1968 Jul 23;161(2):554–557. doi: 10.1016/0005-2787(68)90132-9. [DOI] [PubMed] [Google Scholar]
  40. Batterham T. J., Ghambeer R. K., Blakley R. L., Brownson C. Cobamides and ribonucleotide reduction. IV. Sterochemistry of hydrogen transfer to the deoxyribonucleotide. Biochemistry. 1967 Apr;6(4):1203–1208. doi: 10.1021/bi00856a033. [DOI] [PubMed] [Google Scholar]
  41. Beacham I. R. A new assay for phosphodeoxyribomutase: surface localisation of the enzyme. Biochim Biophys Acta. 1969 Sep 30;191(1):158–161. doi: 10.1016/0005-2744(69)90325-8. [DOI] [PubMed] [Google Scholar]
  42. Beacham I. R., Barth P. T., Pritchard R. H. Constitutivity of thymidine phosphorylase in deoxyriboaldolase negative strains: dependence on thymine requirement and concentration. Biochim Biophys Acta. 1968 Sep 24;166(2):589–592. doi: 10.1016/0005-2787(68)90251-7. [DOI] [PubMed] [Google Scholar]
  43. Beacham I. R., Eisenstark A., Barth P. T., Pritchard R. H. Deoxynucleoside-sensitive mutants of Salmonella typhimurium. Mol Gen Genet. 1968;102(2):112–127. doi: 10.1007/BF01789138. [DOI] [PubMed] [Google Scholar]
  44. Beck W. S., Goulian M., Larsson A., Reichard P. Hydrogen donor specificity of cobamide-dependent ribonucleotide reductase and allosteric regulation of substrate specificity. J Biol Chem. 1966 May 10;241(9):2177–2179. [PubMed] [Google Scholar]
  45. Beck W. S., Hardy J. Requirement of ribonucleotide reductase for cobamide coenzyme, a product of ribosomal activity. Proc Natl Acad Sci U S A. 1965 Jul;54(1):286–293. doi: 10.1073/pnas.54.1.286. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Beck W. S. Regulation of cobamide-dependent ribonucleotide reductase by allosteric effectors and divalent cations. J Biol Chem. 1967 Jul 10;242(13):3148–3158. [PubMed] [Google Scholar]
  47. Berglund O. Identification of a thioredoxin induced by bacteriophage T4. J Biol Chem. 1969 Nov 25;244(22):6306–6308. [PubMed] [Google Scholar]
  48. Berglund O., Karlström O., Reichard P. A new ribonucleotide reductase system after infection with phage T4. Proc Natl Acad Sci U S A. 1969 Mar;62(3):829–835. doi: 10.1073/pnas.62.3.829. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Bernofsky C., Utter M. F. Secondary activation effects of mitochondrial isocitrate dehydrogenases from yeast. Biochim Biophys Acta. 1967 Mar 15;132(2):244–255. doi: 10.1016/0005-2744(67)90143-x. [DOI] [PubMed] [Google Scholar]
  50. Bethell M. R., Jones M. E. Molecular size and feedback-regulation characteristics of bacterial asartate transcarbamulases. Arch Biochem Biophys. 1969 Nov;134(2):352–365. doi: 10.1016/0003-9861(69)90294-x. [DOI] [PubMed] [Google Scholar]
  51. Bethell M. R., Smith K. E., White J. S., Jones M. E. Carbamyl phosphate: an allosteric substrate for aspartate transcarbamylase of Escherichia coli. Proc Natl Acad Sci U S A. 1968 Aug;60(4):1442–1449. doi: 10.1073/pnas.60.4.1442. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Blakley R. L. B12-dependent synthesis of deoxyribonucleotides. Fed Proc. 1966 Nov-Dec;25(6):1633–1638. [PubMed] [Google Scholar]
  53. Blakley R. L., Barker H. A. Cobamide stimulation of the reduction of ribotides to deoxyribotides in Lactobacillus leichmannii. Biochem Biophys Res Commun. 1964 Jul 27;16(5):391–397. doi: 10.1016/0006-291x(64)90363-8. [DOI] [PubMed] [Google Scholar]
  54. Blakley R. L., Ghambeer R. K., Batterham T. J., Brownson C. Studies with hydrogen isotopes on the mechanism of action of cobamide-dependent ribonucleotide reductase. Biochem Biophys Res Commun. 1966 Aug 12;24(3):418–426. doi: 10.1016/0006-291x(66)90176-8. [DOI] [PubMed] [Google Scholar]
  55. Blakley R. L., Ghambeer R. K., Nixon P. F., Vitols E. The cobamide-dependent ribonucleoside triphosphate reductase of lactobacilli. Biochem Biophys Res Commun. 1965 Aug 16;20(4):439–445. doi: 10.1016/0006-291x(65)90597-8. [DOI] [PubMed] [Google Scholar]
  56. Blakley R. L., Vitols E. The control of nucleotide biosynthesis. Annu Rev Biochem. 1968;37:201–224. doi: 10.1146/annurev.bi.37.070168.001221. [DOI] [PubMed] [Google Scholar]
  57. Bolton E. BIOSYNTHESIS OF NUCLEIC ACID IN ESCHERICHIA COLI. Proc Natl Acad Sci U S A. 1954 Aug;40(8):764–772. doi: 10.1073/pnas.40.8.764. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Breitman T. R., Bradford R. M., Cannon W. D., Jr Use of exogenous deoxythymidylic acid to label the deoxyribonucleic acid of growing wild-type Escherichia coli. J Bacteriol. 1967 Apr;93(4):1471–1472. doi: 10.1128/jb.93.4.1471-1472.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  59. Breitman T. R., Bradford R. M. Inability of low thymine-requiring mutants of Escherichia coli lacking phosphodeoxyribomutase to be induced for deoxythymidine phosphorylase and deoxyriboaldolase. J Bacteriol. 1968 Jun;95(6):2434–2435. doi: 10.1128/jb.95.6.2434-2435.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  60. Breitman T. R., Bradford R. M. Metabolism of thymineless mutants of Escherichia coli. I. Absence of thymidylate synthetase activity and growth characteristics of two sequential thymineless mutants. J Bacteriol. 1967 Mar;93(3):845–852. doi: 10.1128/jb.93.3.845-852.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  61. Breitman T. R., Bradford R. M. The absence of deoxyriboaldolase activity in a thymineless mutant of Escherichia coli strain 15: a possible explanation for the low thymine requirement of some thymineless strains. Biochim Biophys Acta. 1967 Mar 29;138(1):217–220. doi: 10.1016/0005-2787(67)90610-7. [DOI] [PubMed] [Google Scholar]
  62. Brown N. C., Canellakis Z. N., Lundin B., Reichard P., Thelander L. Ribonucleoside diphosphate reductase. Purification of the two subunits, proteins B1 and B2. Eur J Biochem. 1969 Jul;9(4):561–573. doi: 10.1111/j.1432-1033.1969.tb00646.x. [DOI] [PubMed] [Google Scholar]
  63. Brown N. C., Eliasson R., Reichard P., Thelander L. Spectrum and iron content of protein B2 from ribonucleoside diphosphate reductase. Eur J Biochem. 1969 Jul;9(4):512–518. doi: 10.1111/j.1432-1033.1969.tb00639.x. [DOI] [PubMed] [Google Scholar]
  64. Brown N. C., Reichard P. Ribonucleoside diphosphate reductase. Formation of active and inactive complexes of proteins B1 and B2. J Mol Biol. 1969 Nov 28;46(1):25–38. doi: 10.1016/0022-2836(69)90055-2. [DOI] [PubMed] [Google Scholar]
  65. Brown N. C., Reichard P. Role of effector binding in allosteric control of ribonucleoside diphosphate reductase. J Mol Biol. 1969 Nov 28;46(1):39–55. doi: 10.1016/0022-2836(69)90056-4. [DOI] [PubMed] [Google Scholar]
  66. Budman D. R., Pardee A. B. Thymidine and thymine incorporation into deoxyribonucleic acid: inhibition and repression by uridine of thymidine phosphorylase of Escherichia coli. J Bacteriol. 1967 Nov;94(5):1546–1550. doi: 10.1128/jb.94.5.1546-1550.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. CHAKRABORTY K. P., HURLBERT R. B. Role of glutamine in the biosynthesis of cytidine nucleotides in Escherichia coli. Biochim Biophys Acta. 1961 Mar 4;47:607–609. doi: 10.1016/0006-3002(61)90563-7. [DOI] [PubMed] [Google Scholar]
  68. CHARLES H. P. Response of Neurospora mutants to carbon dioxide. Nature. 1962 Jul 28;195:359–360. doi: 10.1038/195359a0. [DOI] [PubMed] [Google Scholar]
  69. CIHAK A., SORM F. INHIBITION BY 5-AZAURACIL OF THE URIDINE PHOSPHORYLASE AND DEOXYURIDINE PHOSPHORYLASE ACTIVITIES IN CELL-FREE EXTRACT OF MOUSE LIVER. Biochim Biophys Acta. 1964 Apr 27;80:672–674. [PubMed] [Google Scholar]
  70. COHEN G. N., PATTE J. C., TRUFFA-BACHI P. PARALLEL MODIFICATIONS CAUSED BY MUTATIONS IN TWO ENZYMES CONCERNED WITH THE BIOSYNTHESIS OF THREONINE IN ESCHERICHIA COLI. Biochem Biophys Res Commun. 1965 May 3;19:546–550. doi: 10.1016/0006-291x(65)90160-9. [DOI] [PubMed] [Google Scholar]
  71. COHEN S. S., BARNER H. D. The conversion of 5-methyldeoxycytidine to thymidine in vitro and in vivo. J Biol Chem. 1957 Jun;226(2):631–642. [PubMed] [Google Scholar]
  72. COHEN S. S. On biochemical variability and innovation. Science. 1963 Mar 15;139(3559):1017–1026. doi: 10.1126/science.139.3559.1017. [DOI] [PubMed] [Google Scholar]
  73. COHEN S. S. Studies on controlling mechanisms in the metabolism of virus-infected bacteria. Cold Spring Harb Symp Quant Biol. 1953;18:221–235. doi: 10.1101/sqb.1953.018.01.033. [DOI] [PubMed] [Google Scholar]
  74. CRAWFORD I., KORNBERG A., SIMMS E. S. Conversion of uracil and orotate to uridine 5'-phosphate by enzymes in lactobacilli. J Biol Chem. 1957 Jun;226(2):1093–1101. [PubMed] [Google Scholar]
  75. CRAWFORD L. V. Thymine metabolism in strains of Escherichia coli. Biochim Biophys Acta. 1958 Nov;30(2):428–429. doi: 10.1016/0006-3002(58)90071-4. [DOI] [PubMed] [Google Scholar]
  76. CREASEY W. A., HANDSCHUMACHER R. E. Purification and properties of orotidylate decarboxylases from yeast and rat liver. J Biol Chem. 1961 Jul;236:2058–2063. [PubMed] [Google Scholar]
  77. Cannon W. D., Jr, Breitman T. R. Control of deoxynucleotide biosynthesis in Escherichia coli. I. Decrease of pyrimidine deoxynucleotide biosynthesis in vivo in the presence of deoxythymidylate. Biochemistry. 1967 Mar;6(3):810–816. doi: 10.1021/bi00855a022. [DOI] [PubMed] [Google Scholar]
  78. Cannon W. D., Jr, Breitman T. R. Control of deoxynucleotide biosynthesis in Escherichia coli. II. Effect of deoxythymidylate on the biosynthesis of both deoxynucleotides and ribonucleotide reductase. Arch Biochem Biophys. 1968 Sep 20;127(1):534–542. doi: 10.1016/0003-9861(68)90259-2. [DOI] [PubMed] [Google Scholar]
  79. Caroline D. F., Davis R. H. Pyrimidine synthesis in Neurospora crassa: regulation of enzyme activities. J Bacteriol. 1969 Dec;100(3):1378–1384. doi: 10.1128/jb.100.3.1378-1384.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  80. Caroline D. F. Pyrimidine synthesis in Neurospora crassa: gene-enzyme relationships. J Bacteriol. 1969 Dec;100(3):1371–1377. doi: 10.1128/jb.100.3.1371-1377.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  81. Changeux J. P., Gerhart J. C., Schachman H. K. Allosteric interactions in aspartate transcarbamylase. I. Binding of specific ligands to the native enzyme and its isolated subunits. Biochemistry. 1968 Feb;7(2):531–538. doi: 10.1021/bi00842a007. [DOI] [PubMed] [Google Scholar]
  82. Cihák A., Sorm F. Metabolic transformations of 5-azaorotate: cause of marked inhibition of orotidine-5'-phosphate decarboxylase. Biochim Biophys Acta. 1967 Nov 21;149(1):314–316. [PubMed] [Google Scholar]
  83. Cohen S. S., Barner H. D. STUDIES ON UNBALANCED GROWTH IN ESCHERICHIA COLI. Proc Natl Acad Sci U S A. 1954 Oct;40(10):885–893. doi: 10.1073/pnas.40.10.885. [DOI] [PMC free article] [PubMed] [Google Scholar]
  84. Cohen S. S., Flaks J. G., Barner H. D., Loeb M. R., Lichtenstein J. THE MODE OF ACTION OF 5-FLUOROURACIL AND ITS DERIVATIVES. Proc Natl Acad Sci U S A. 1958 Oct 15;44(10):1004–1012. doi: 10.1073/pnas.44.10.1004. [DOI] [PMC free article] [PubMed] [Google Scholar]
  85. Cohen S. S. Introduction to the biochemistry of D-arabinosyl nucleosides. Prog Nucleic Acid Res Mol Biol. 1966;5:1–88. doi: 10.1016/s0079-6603(08)60231-7. [DOI] [PubMed] [Google Scholar]
  86. Collins K. D., Stark G. R. Aspartate transcarbamylase. Studies of the catalytic subunit by ultraviolet difference spectroscopy. J Biol Chem. 1969 Apr 10;244(7):1869–1877. [PubMed] [Google Scholar]
  87. Colowick S. P., Womack F. C. Binding of diffusible molecules by macromolecules: rapid measurement by rate of dialysis. J Biol Chem. 1969 Feb 25;244(4):774–777. [PubMed] [Google Scholar]
  88. Cowles J. R., Evans H. J., Russell S. A. B12 coenzyme-dependent ribonucleotide reductase in Rhizobium species and the effects of cobalt deficiency on the activity of the enzyme. J Bacteriol. 1969 Mar;97(3):1460–1465. doi: 10.1128/jb.97.3.1460-1465.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  89. Cowles J. R., Evans H. J. Some properties of the ribonucleotide reductase from Rhizobium meliloti. Arch Biochem Biophys. 1968 Sep 20;127(1):770–778. doi: 10.1016/0003-9861(68)90288-9. [DOI] [PubMed] [Google Scholar]
  90. Cummings D. J., Mondale L. Thymineless death in Escherichia coli: strain specificity. J Bacteriol. 1967 Jun;93(6):1917–1924. doi: 10.1128/jb.93.6.1917-1924.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  91. DATTA P., GEST H. HOMOSERINE DEHYDROGENASE OF RHODOSPIRILLUM RUBRUM. PURIFICATION, PROPERTIES, AND FEEDBACK CONTROL OF ACTIVITY. J Biol Chem. 1965 Jul;240:3023–3033. [PubMed] [Google Scholar]
  92. DAVIS R. H. Consequences of a suppressor gene effective with pyrimidine and proline mutants of Neurospora. Genetics. 1962 Mar;47:351–360. doi: 10.1093/genetics/47.3.351. [DOI] [PMC free article] [PubMed] [Google Scholar]
  93. DAVIS R. H. NEUROSPORA MUTANT LACKING AN ARGININE-SPECIFIC CARBAMYL PHOSPHOKINASE. Science. 1963 Dec 27;142(3600):1652–1654. doi: 10.1126/science.142.3600.1652. [DOI] [PubMed] [Google Scholar]
  94. DAVIS R. H. Suppressor of pyrimidine 3 mutants of Neurospora and its relation to arginine synthesis. Science. 1961 Aug 18;134(3477):470–471. doi: 10.1126/science.134.3477.470. [DOI] [PubMed] [Google Scholar]
  95. DAVIS R. H., WOODWARD V. W. The relationship between gene suppression and aspartate transcarbamylase activity in pyr-3 mutants of Neurospora. Genetics. 1962 Aug;47:1075–1083. doi: 10.1093/genetics/47.8.1075. [DOI] [PMC free article] [PubMed] [Google Scholar]
  96. DONACHIE W. D. THE REGULATION OF PYRIMIDINE BIOSYNTHESIS IN NEUROSPORA CRASSA. I. END-PRODUCT INHIBITION AND REPRESSION OF ASPARTATE CARBAMOYLTRANSFERASE. Biochim Biophys Acta. 1964 Feb 10;82:284–292. doi: 10.1016/0304-4165(64)90299-5. [DOI] [PubMed] [Google Scholar]
  97. Dale B., Greenberg G. R. Genetic mapping of a mutation in Escherichia coli showing reduced activity of thymidine phosphorylase. J Bacteriol. 1967 Sep;94(3):778–779. doi: 10.1128/jb.94.3.778-779.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  98. Davis R. H. AN ENZYMATIC DIFFERENCE AMONG PYR-3 MUTANTS OF NEUROSPORA CRASSA. Proc Natl Acad Sci U S A. 1960 May;46(5):677–682. doi: 10.1073/pnas.46.5.677. [DOI] [PMC free article] [PubMed] [Google Scholar]
  99. Davis R. H. Carbamyl phosphate synthesis in Neurospora crassa. II. Genetics, metabolic position, and regulation of arginine-specific carbamyl phosphokinase. Biochim Biophys Acta. 1965 Aug 24;107(1):54–68. doi: 10.1016/0304-4165(65)90388-0. [DOI] [PubMed] [Google Scholar]
  100. Denhardt D. T. Formation of ribosylthymine in Escherichia coli. Studies on pulse labeling with thymine and thymidine. J Biol Chem. 1969 May 25;244(10):2710–2715. [PubMed] [Google Scholar]
  101. Dennis P. P., Herman R. K. Pyrimidine pools and macromolecular composition of pyrimidine-limited Escherichia coli. J Bacteriol. 1970 Apr;102(1):118–123. doi: 10.1128/jb.102.1.118-123.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  102. Eakin R. T., Mitchell H. K. A mitochondrial dihydroorotate oxidase system in Neurospora crassa. Arch Biochem Biophys. 1969 Oct;134(1):160–171. doi: 10.1016/0003-9861(69)90262-8. [DOI] [PubMed] [Google Scholar]
  103. Edlin G., Stent G. S. Nucleoside triphosphate pools and the regulation of RNA synthesis in E. coli. Proc Natl Acad Sci U S A. 1969 Feb;62(2):475–482. doi: 10.1073/pnas.62.2.475. [DOI] [PMC free article] [PubMed] [Google Scholar]
  104. Eisenstark A., Eisenstark R., Cunningham S. Genetic analysis of thymineless(thy) mutants in Salmonella typhimurium. Genetics. 1968 Apr;58(4):493–506. doi: 10.1093/genetics/58.4.493. [DOI] [PMC free article] [PubMed] [Google Scholar]
  105. Elford H. L. Effect of hydroxyurea on ribonucleotide reductase. Biochem Biophys Res Commun. 1968 Oct 10;33(1):129–135. doi: 10.1016/0006-291x(68)90266-0. [DOI] [PubMed] [Google Scholar]
  106. FARMER J. L., ROTHMAN F. TRANSFORMABLE THYMINE-REQUIRING MUTANT OF BACILLUS SUBTILS. J Bacteriol. 1965 Jan;89:262–263. doi: 10.1128/jb.89.1.262-263.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  107. FINK R. M., FINK K. Biosynthesis of radioactive RNA and DNA pyrimidines from thymidine-2-C-14. Biochem Biophys Res Commun. 1961 Oct 23;6:7–10. doi: 10.1016/0006-291x(61)90174-7. [DOI] [PubMed] [Google Scholar]
  108. FINK R. M., FINK K. Relative retention of H3 and C14 labels of nucleosides incorporated into nucleic acids of Neurospora. J Biol Chem. 1962 Sep;237:2889–2891. [PubMed] [Google Scholar]
  109. FINK R. M., FINK K. Utilization of radiocarbon from thymidine and other precursors of ribonucleic acid in Neurospora crassa. J Biol Chem. 1962 Jul;237:2289–2290. [PubMed] [Google Scholar]
  110. FLAKS J. G., COHEN S. S. The enzymic synthesis of 5-hydroxymethyldeoxycytidylic acid. Biochim Biophys Acta. 1957 Sep;25(3):667–668. doi: 10.1016/0006-3002(57)90553-x. [DOI] [PubMed] [Google Scholar]
  111. FRIEDKIN M., CRAWFORD E. J., DONOVAN E., PASTORE E. J. The enzymatic synthesis of thymidylate. III. The further purification of thymidylate synthetase and its separation from natural fluorescent inhibitors. J Biol Chem. 1962 Dec;237:3811–3814. [PubMed] [Google Scholar]
  112. FRIEDMANN H. C., VENNESLAND B. Crystalline dihydroorotic dehydrogenase. J Biol Chem. 1960 May;235:1526–1532. [PubMed] [Google Scholar]
  113. FRIEDMANN H. C., VENNESLAND B. Purification and properties of dihydro-orotic dehydrogenase. J Biol Chem. 1958 Dec;233(6):1398–1406. [PubMed] [Google Scholar]
  114. Fangman W. L., Novick A. Mutant bacteria showing efficient utilization of thymidine. J Bacteriol. 1966 Jun;91(6):2390–2391. doi: 10.1128/jb.91.6.2390-2391.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  115. Fangman W. L. Specificity and efficiency of thymidine incorporation in Escherichia coli lacking thymidine phosphorylase. J Bacteriol. 1969 Sep;99(3):681–687. doi: 10.1128/jb.99.3.681-687.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  116. Finck D., Suyama Y., Davis R. H. Metabolic role of the pyrimidine-3 locus of Neurospora. Genetics. 1965 Oct;52(4):829–834. doi: 10.1093/genetics/52.4.829. [DOI] [PMC free article] [PubMed] [Google Scholar]
  117. Fink G. R., Roth J. R. Histidine regulatory mutants in Salmonella typhiumium. VI. Dominance studies. J Mol Biol. 1968 May 14;33(3):547–557. doi: 10.1016/0022-2836(68)90305-7. [DOI] [PubMed] [Google Scholar]
  118. Fleming W. H., Bessman M. J. The enzymology of virus-infected bacteria. IX. Purification and properties of the deoxycytidylate deaminase of T6-infected Escherichia coli. J Biol Chem. 1967 Feb 10;242(3):363–371. [PubMed] [Google Scholar]
  119. Follmann H., Hogenkamp H. P. Ribonucleotide reductases. Studies with 18-O-labeled substrates. Biochemistry. 1969 Nov;8(11):4372–4375. doi: 10.1021/bi00839a022. [DOI] [PubMed] [Google Scholar]
  120. Furth J. J., Cohen S. S. Inhibition of mammalian DNA polymerase by the 5'-triphosphate of 1-beta-d-arabinofuranosylcytosine and the 5'-triphosphate of 9-beta-d-arabinofuranoxyladenine. Cancer Res. 1968 Oct;28(10):2061–2067. [PubMed] [Google Scholar]
  121. GERHART J. C., PARDEE A. B. ASPARTATE TRANSCARBAMYLASE, AN ENZYME DESIGNED FOR FEEDBACK INHIBITION. Fed Proc. 1964 May-Jun;23:727–735. [PubMed] [Google Scholar]
  122. GERHART J. C., PARDEE A. B. The enzymology of control by feedback inhibition. J Biol Chem. 1962 Mar;237:891–896. [PubMed] [Google Scholar]
  123. GERHART J. C. SUBUNITS FOR CONTROL AND CATALYSIS IN ASPARTATE TRANSCARBAMYLASE. Brookhaven Symp Biol. 1964 Dec;17:222–231. [PubMed] [Google Scholar]
  124. GORINI L., GUNDERSEN W., BURGER M. Genetics of regulation of enzyme synthesis in the arginine biosynthetic pathway of Escherichia coli. Cold Spring Harb Symp Quant Biol. 1961;26:173–182. doi: 10.1101/sqb.1961.026.01.022. [DOI] [PubMed] [Google Scholar]
  125. GREENBERG G. R., SOMERVILLE R. L. Deoxyuridylate kinase activity and deoxyuridinetriphosphatase in Escherichia coli. Proc Natl Acad Sci U S A. 1962 Feb;48:247–257. doi: 10.1073/pnas.48.2.247. [DOI] [PMC free article] [PubMed] [Google Scholar]
  126. Gardner R., Kornberg A. Biochemical studies of bacterial sporulation and germination. V. Purine nucleoside phosphorylase of vegetative cells and spores of Bacillus cereus. J Biol Chem. 1967 May 25;242(10):2383–2388. [PubMed] [Google Scholar]
  127. Gerhart J. C., Holoubek H. The purification of aspartate transcarbamylase of Escherichia coli and separation of its protein subunits. J Biol Chem. 1967 Jun 25;242(12):2886–2892. [PubMed] [Google Scholar]
  128. Gerhart J. C., Schachman H. K. Allosteric interactions in aspartate transcarbamylase. II. Evidence for different conformational states of the protein in the presence and absence of specific ligands. Biochemistry. 1968 Feb;7(2):538–552. doi: 10.1021/bi00842a600. [DOI] [PubMed] [Google Scholar]
  129. Gerhart J. C., Schachman H. K. Distinct subunits for the regulation and catalytic activity of aspartate transcarbamylase. Biochemistry. 1965 Jun;4(6):1054–1062. doi: 10.1021/bi00882a012. [DOI] [PubMed] [Google Scholar]
  130. Ghambeer R. K., Blakley R. L. Cobamides and ribonucleotide reduction. 3. Factors influencing the level of cobamide-dependent ribonucleoside triphosphate reductase in Lactobacillus leichmannii. J Biol Chem. 1966 Oct 25;241(20):4710–4716. [PubMed] [Google Scholar]
  131. Ghambeer R. K., Blakley R. L. Factors influencing the level of cobamide-dependent ribonucleoside triphosphate reductase in Lactobacillus leichmannii. Biochem Biophys Res Commun. 1965 Oct 8;21(1):40–48. doi: 10.1016/0006-291x(65)90423-7. [DOI] [PubMed] [Google Scholar]
  132. Ginsberg T., David F. F. The biosynthesis of pseudouridine in ribonucleic acids of Escherichia coli. J Biol Chem. 1968 Dec 10;243(23):6300–6305. [PubMed] [Google Scholar]
  133. Gottesman M. M., Beck W. S. Transfer of hydrogen in the cobamide-dependent ribonucleotide reductase reaction. Biochem Biophys Res Commun. 1966 Aug 12;24(3):353–359. doi: 10.1016/0006-291x(66)90163-x. [DOI] [PubMed] [Google Scholar]
  134. Goulian M., Beck W. S. Purification and properties of cobamide-dependent ribonucleotide reductase from Lactobacillus leichmannii. J Biol Chem. 1966 Sep 25;241(18):4233–4242. [PubMed] [Google Scholar]
  135. Greenberg G. R. New dUTPase and dUDPase activites after infection of Escherichia coli by T2 bacteriophage. Proc Natl Acad Sci U S A. 1966 Oct;56(4):1226–1232. doi: 10.1073/pnas.56.4.1226. [DOI] [PMC free article] [PubMed] [Google Scholar]
  136. Grenson M. The utilization of exogenous pyrimidines and the recycling of uridine-5'-phosphate derivatives in Saccharomyces cerevisiae, as studied by means of mutants affected in pyrimidine uptake and metabolism. Eur J Biochem. 1969 Dec;11(2):249–260. doi: 10.1111/j.1432-1033.1969.tb00767.x. [DOI] [PubMed] [Google Scholar]
  137. Griffin C. E., Hamilton F. D., Hopper S. P., Abrams R. Stereospecificity of deoxycytidine triphosphate synthesis with the ribonucleotide reductase of Lactobacillus leichmanii. Arch Biochem Biophys. 1968 Sep 10;126(3):905–911. doi: 10.1016/0003-9861(68)90484-0. [DOI] [PubMed] [Google Scholar]
  138. Grivell A. R., Jackson J. F. Thymidine kinase: evidence for its absence from Neurospora crassa and some other micro-organisms, and the relevance of this to the specific labelling of deoxyribonucleic acid. J Gen Microbiol. 1968 Dec;54(2):307–317. doi: 10.1099/00221287-54-2-307. [DOI] [PubMed] [Google Scholar]
  139. Gross S. R. The regulation of synthesis of leucine biosynthetic enzymes in Neurospora. Proc Natl Acad Sci U S A. 1965 Dec;54(6):1538–1546. doi: 10.1073/pnas.54.6.1538. [DOI] [PMC free article] [PubMed] [Google Scholar]
  140. Gutnick D., Calvo J. M., Klopotowski T., Ames B. N. Compounds which serve as the sole source of carbon or nitrogen for Salmonella typhimurium LT-2. J Bacteriol. 1969 Oct;100(1):215–219. doi: 10.1128/jb.100.1.215-219.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  141. HANDSCHUMACHER R. E. Orotidylic acid decarboxylase: inhibition studies with azauridine 5'-phosphate. J Biol Chem. 1960 Oct;235:2917–2919. [PubMed] [Google Scholar]
  142. HANDSCHUMACHER R. E., PASTERNAK C. A. Inhibition of orotidylic acid decarboxylase, a primary site of carcinostasis by 6-azauracil. Biochim Biophys Acta. 1958 Nov;30(2):451–452. doi: 10.1016/0006-3002(58)90088-x. [DOI] [PubMed] [Google Scholar]
  143. HANDSCHUMACHER R. E. Studies of bacterial resistance to 6-azauracil and its riboside. Biochim Biophys Acta. 1957 Feb;23(2):428–430. doi: 10.1016/0006-3002(57)90348-7. [DOI] [PubMed] [Google Scholar]
  144. HANDSCHUMACHER R. E., WELCH A. D. Microbial studies of 6-azauracil, an antagonist of uracil. Cancer Res. 1956 Nov;16(10 Pt 1):965–969. [PubMed] [Google Scholar]
  145. HAYAISHI O., KORNBERG A. Metabolism of cytosine, thymine, uracil, and barbituric acid by bacterial enzymes. J Biol Chem. 1952 May;197(2):717–732. [PubMed] [Google Scholar]
  146. HOFFMANN C. E., LAMPEN J. O. Products of desoxyribose degradation by Escherichia coli. J Biol Chem. 1952 Oct;198(2):885–893. [PubMed] [Google Scholar]
  147. HOLMES W. L. Studies on the mode of action of analogues of orotic acid; 6-uracilsulfonic acid, 6-uracilsulfonamide, and 6-uracil methyl sulfone. J Biol Chem. 1956 Dec;223(2):677–686. [PubMed] [Google Scholar]
  148. HURLBERT R. B., POTTER V. R. A survey of the metabolism of orotic acid in the rat. J Biol Chem. 1952 Mar;195(1):257–270. [PubMed] [Google Scholar]
  149. Hager S. E., Jones M. E. A glutamine-dependent enzyme for the synthesis of carbamyl phosphate for pyrimidine biosynthesis in fetal rat liver. J Biol Chem. 1967 Dec 25;242(24):5674–5680. [PubMed] [Google Scholar]
  150. Hamilton J. A., Blakley R. L. Electron spin resonance studies of ribonucleotide reduction catalyzed by the ribonucleotide eductase of Lactobacillus leichmannii. Biochim Biophys Acta. 1969 Jun 17;184(1):224–226. doi: 10.1016/0304-4165(69)90123-8. [DOI] [PubMed] [Google Scholar]
  151. Hamilton J. A., Blakley R. L., Looney F. D., Winfield M. E. Formation of a cobamide containing divalent cobalt by the ribonucleotide reductase of Lactobacillus leichmanii. Biochim Biophys Acta. 1969 Apr 1;177(2):374–376. doi: 10.1016/0304-4165(69)90155-x. [DOI] [PubMed] [Google Scholar]
  152. Harrison A. P., Jr Thymine incorporation and metabolism by various classes of thymine-less bacteria. J Gen Microbiol. 1965 Dec;41(3):321–333. doi: 10.1099/00221287-41-3-321. [DOI] [PubMed] [Google Scholar]
  153. Hayward W. S., Belser W. L. Regulation of pyrimidine biosynthesis in Serratia marcescens. Proc Natl Acad Sci U S A. 1965 Jun;53(6):1483–1489. doi: 10.1073/pnas.53.6.1483. [DOI] [PMC free article] [PubMed] [Google Scholar]
  154. Hill A. V. The Combinations of Haemoglobin with Oxygen and with Carbon Monoxide. I. Biochem J. 1913 Oct;7(5):471–480. doi: 10.1042/bj0070471. [DOI] [PMC free article] [PubMed] [Google Scholar]
  155. Hiraga S., Igarashi K., Yura T. A deoxythymidine kinase-deficient mutant of Escherichia coli. I. Isolation and some properties. Biochim Biophys Acta. 1967 Aug 22;145(1):41–51. doi: 10.1016/0005-2787(67)90652-1. [DOI] [PubMed] [Google Scholar]
  156. Hoffee P. A. 2-deoxyribose gene-enzyme complex in Salmonella typhimurium. I. Isolation and enzymatic characterization of 2-deoxyribose-negative mutants. J Bacteriol. 1968 Feb;95(2):449–457. doi: 10.1128/jb.95.2.449-457.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  157. Hoffee P. A. 2-deoxyribose-5-phosphate aldolase of Salmonella typhimurium: purification and properties. Arch Biochem Biophys. 1968 Sep 10;126(3):795–802. doi: 10.1016/0003-9861(68)90473-6. [DOI] [PubMed] [Google Scholar]
  158. Hoffee P. A., Robertson B. C. 2-Deoxyribose gene-enzyme complex in Salmonella typhimurium: regulation of phosphodeoxyribomutase. J Bacteriol. 1969 Mar;97(3):1386–1396. doi: 10.1128/jb.97.3.1386-1396.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  159. Hogenkamp H. P., Ghambeer R. K., Brownson C., Blakley R. L., Vitols E. Cobamides and ribonucleotide reduction. VI. Enzyme-catalyzed hydrogen exchange between water and deoxyadenosylcobalamin. J Biol Chem. 1968 Feb 25;243(4):799–808. [PubMed] [Google Scholar]
  160. Holmgren A., Perham R. N., Baldesten A. Thioredoxin. 3. Amino acid sequences of the peptic peptides from S-aminoethylated peptide B. Eur J Biochem. 1968 Aug;5(3):352–358. doi: 10.1111/j.1432-1033.1968.tb00377.x. [DOI] [PubMed] [Google Scholar]
  161. Holmgren A., Reichard P. Thioredoxin 2: cleavage with cyanogen bromide. Eur J Biochem. 1967 Sep;2(2):187–196. doi: 10.1111/j.1432-1033.1967.tb00125.x. [DOI] [PubMed] [Google Scholar]
  162. Holmgren A. Thioredoxin. 4. Amino acid sequence of peptide B. Eur J Biochem. 1968 Aug;5(3):359–365. doi: 10.1111/j.1432-1033.1968.tb00378.x. [DOI] [PubMed] [Google Scholar]
  163. Holmgren A. Thioredoxin. 5. Amino acid sequences of the tryptic peptides of peptide A. Eur J Biochem. 1968 Dec 5;6(4):467–474. doi: 10.1111/j.1432-1033.1968.tb00469.x. [DOI] [PubMed] [Google Scholar]
  164. Honzová H., Javůrková B., Skoda J., Dyr J. A quantitative evaluation of the mutagenic effect of ethylmethanesulfonate in Brevibacterium ammoniagenes and qualitative character of the mutants obtained. Folia Microbiol (Praha) 1968;13(2):125–128. doi: 10.1007/BF02868212. [DOI] [PubMed] [Google Scholar]
  165. Hutson J. Y., Downing M. Pyrimidine biosynthesis in Lactobacillus leichmannii. J Bacteriol. 1968 Oct;96(4):1249–1254. doi: 10.1128/jb.96.4.1249-1254.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  166. ISHIBASHI M., SUGINO Y., HIROTA Y. CHROMOSOMAL LOCATION OF THYMINE AND ARGININE GENES IN ESCHERICHIA COLI AND AN F' INCORPORATING THEM. J Bacteriol. 1964 Mar;87:554–561. doi: 10.1128/jb.87.3.554-561.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  167. Igarashi K., Hiraga S., Yura T. A deoxythymidine kinase deficient mutant of Escherichia coli. II. Mapping and transduction studies with phage phi 80. Genetics. 1967 Nov;57(3):643–654. doi: 10.1093/genetics/57.3.643. [DOI] [PMC free article] [PubMed] [Google Scholar]
  168. Imada A., Igarasi S. Ribosyl and deoxyribosyl transfer by bacterial enzyme systems. J Bacteriol. 1967 Nov;94(5):1551–1559. doi: 10.1128/jb.94.5.1551-1559.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  169. Isaac J. H., Holloway B. W. Control of pyrimidine biosynthesis in Pseudomonas aeruginosa. J Bacteriol. 1968 Nov;96(5):1732–1741. doi: 10.1128/jb.96.5.1732-1741.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  170. Issaly I. M., Issaly A. S., Reissig J. L. Carbamyl phosphate biosynthesis in Bacillus subtilis. Biochim Biophys Acta. 1970 Mar 18;198(3):482–494. doi: 10.1016/0005-2744(70)90126-9. [DOI] [PubMed] [Google Scholar]
  171. Iwatsuki N., Okazaki R. Mechanism of regulation of deoxythymidine kinase of Escherichia coli. I. Effect of regulatory deoxynucleotides on the state of aggregation of the enzyme. J Mol Biol. 1967 Oct 14;29(1):139–154. doi: 10.1016/0022-2836(67)90186-6. [DOI] [PubMed] [Google Scholar]
  172. Iwatsuki N., Okazaki R. Mechanism of regulation of deoxythymidine kinase of Escherichia coli. II. Effect of temperature on the enzyme activity and kinetics. J Mol Biol. 1967 Oct 14;29(1):155–165. doi: 10.1016/0022-2836(67)90187-8. [DOI] [PubMed] [Google Scholar]
  173. KITSUJI N. THYMINELESS MUTATION SITE ON ESCHERICHIA COLI CHROMOSOME. J Bacteriol. 1964 Apr;87:802–808. doi: 10.1128/jb.87.4.802-808.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  174. KOCH A. L. Some enzymes of nucleoside metabolism of Escherichia coli. J Biol Chem. 1956 Nov;223(1):535–549. [PubMed] [Google Scholar]
  175. KOERNER J. F., SMITH M. S., BUCHANAN J. M. Deoxycytidine triphosphatase, an enzyme induced by bacteriophage infection. J Biol Chem. 1960 Sep;235:2691–2697. [PubMed] [Google Scholar]
  176. KORNBERG A., LIEBERMAN I., SIMMS E. S. Enzymatic synthesis and properties of 5-phosphoribosylpyrophosphate. J Biol Chem. 1955 Jul;215(1):389–402. [PubMed] [Google Scholar]
  177. KREBS H. A., HEMS R. Some reactions of adenosine and inosine phosphates in animal tissues. Biochim Biophys Acta. 1953 Sep-Oct;12(1-2):172–180. doi: 10.1016/0006-3002(53)90136-x. [DOI] [PubMed] [Google Scholar]
  178. KROOTH R. S. PROPERTIES ODF DIPLOID CELL STRAINS DEVELOPED FROM PATIENTS WITH AN INHERITED ABNORMALITY OF URIDINE BIOSYNTHESIS. Cold Spring Harb Symp Quant Biol. 1964;29:189–212. doi: 10.1101/sqb.1964.029.01.024. [DOI] [PubMed] [Google Scholar]
  179. Kalman S. M., Duffield P. H., Brzozowski T. Purification and properties of a bacterial carbamyl phosphate synthetase. J Biol Chem. 1966 Apr 25;241(8):1871–1877. [PubMed] [Google Scholar]
  180. Kaplan J. G., Duphil M., Lacroute F. A study of the aspartate transcarbamylase activity of yeast. Arch Biochem Biophys. 1967 Mar;119(1):541–551. doi: 10.1016/0003-9861(67)90489-4. [DOI] [PubMed] [Google Scholar]
  181. Kaplan J. G., Lacroute F., Messmer I. On the loss of feedback inhibition of yeast aspartate transcarbamylase during derepression of pyrimidine biosynthesis. Arch Biochem Biophys. 1969 Feb;129(2):539–544. doi: 10.1016/0003-9861(69)90212-4. [DOI] [PubMed] [Google Scholar]
  182. Kaplan J. G., Messmer I. The combined effects of temperature and dilution on the activity and feedback inhibition of yeast aspartate transcarbamylase. Can J Biochem. 1969 Apr;47(4):477–479. doi: 10.1139/o69-074. [DOI] [PubMed] [Google Scholar]
  183. Karlström O., Larsson A. Significance of ribonucleotide reduction in the biosynthesis of deoxyribonucleotides in Escherichia coli. Eur J Biochem. 1967 Dec;3(2):164–170. doi: 10.1111/j.1432-1033.1967.tb19512.x. [DOI] [PubMed] [Google Scholar]
  184. Karlström O. Mutants of Escherichia coli defective in ribonucleoside and deoxyribonucleoside catabolism. J Bacteriol. 1968 Mar;95(3):1069–1077. doi: 10.1128/jb.95.3.1069-1077.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  185. Kerr C. T., Miller R. W. Soluble NADP-linked dihydroorotate dehydrogenase from a pseudomonad. Can J Biochem. 1967 Sep;45(9):1295–1307. doi: 10.1139/o67-151. [DOI] [PubMed] [Google Scholar]
  186. Kirtley M. E., Koshland D. E., Jr Models for cooperative effects in proteins containing subunits. Effects of two interacting ligands. J Biol Chem. 1967 Sep 25;242(18):4192–4205. [PubMed] [Google Scholar]
  187. Koshland D. E., Jr, Némethy G., Filmer D. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry. 1966 Jan;5(1):365–385. doi: 10.1021/bi00865a047. [DOI] [PubMed] [Google Scholar]
  188. Krakoff I. H., Brown N. C., Reichard P. Inhibition of ribonucleoside diphosphate reductase by hydroxyurea. Cancer Res. 1968 Aug;28(8):1559–1565. [PubMed] [Google Scholar]
  189. LACROUTE F., SLONIMSKI P. P. ETUDE PHYSIOLOGIQUE DES MUTANTS R'ESISTANT AU 5-FLUOROURACILE CHEZ LA LEVURE. C R Hebd Seances Acad Sci. 1964 Feb 17;258:2172–2174. [PubMed] [Google Scholar]
  190. LAMPEN J. O., WANG T. P. The mechanism of action of Lactobacillus pentosus nucleosidase. J Biol Chem. 1952 Sep;198(1):385–395. [PubMed] [Google Scholar]
  191. LARSSON A., THELANDER L. THE STEREOSPECIFICITY OF THIOREDOXIN REDUCTASE FOR TRIPHOSPHOPYRIDINE NUCLEOTIDE. J Biol Chem. 1965 Jun;240:2691–2693. [PubMed] [Google Scholar]
  192. LAURENT T. C., MOORE E. C., REICHARD P. ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES. IV. ISOLATION AND CHARACTERIZATION OF THIOREDOXIN, THE HYDROGEN DONOR FROM ESCHERICHIA COLI B. J Biol Chem. 1964 Oct;239:3436–3444. [PubMed] [Google Scholar]
  193. LICHTENSTEIN J., BARNER H. D., COHEN S. S. The metabolism of exogenously supplied nucleotides by Escherichia coli. J Biol Chem. 1960 Feb;235:457–465. [PubMed] [Google Scholar]
  194. LIEBERMAN I. Enzymatic amination of uridine triphosphate to cytidine triphosphate. J Biol Chem. 1956 Oct;222(2):765–775. [PubMed] [Google Scholar]
  195. LIEBERMAN I., KORNBERG A. Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. I. Dihydroortic acid, ureidosuccinic acid, and 5-carboxymethylhydantoin. J Biol Chem. 1954 Apr;207(2):911–924. [PubMed] [Google Scholar]
  196. LIEBERMAN I., KORNBERG A. Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. III. Ureidosuccinase. J Biol Chem. 1955 Feb;212(2):909–920. [PubMed] [Google Scholar]
  197. LIEBERMAN I., KORNBERG A. Enzymic synthesis and breakdown of a pyrimidine, orotic acid. I. Dihydro-orotic dehydrogenase. Biochim Biophys Acta. 1953 Sep-Oct;12(1-2):223–234. doi: 10.1016/0006-3002(53)90141-3. [DOI] [PubMed] [Google Scholar]
  198. LIEBERMAN I., KORNBERG A., SIMMS E. S. Enzymatic synthesis of nucleoside diphosphates and triphosphates. J Biol Chem. 1955 Jul;215(1):429–440. [PubMed] [Google Scholar]
  199. LIEBERMAN I., KORNBERG A., SIMMS E. S. Enzymatic synthesis of pyrimidine nucleotides; orotidine-5'-phosphate and uridine-5'-phosphate. J Biol Chem. 1955 Jul;215(1):403–451. [PubMed] [Google Scholar]
  200. Lacroute F., Piérard A., Grenson M., Wiame J. M. The biosynthesis of carbamoyl phosphate in Saccharomyces cerevisiae. J Gen Microbiol. 1965 Jul;40(1):127–142. doi: 10.1099/00221287-40-1-127. [DOI] [PubMed] [Google Scholar]
  201. Lacroute F. Regulation of pyrimidine biosynthesis in Saccharomyces cerevisiae. J Bacteriol. 1968 Mar;95(3):824–832. doi: 10.1128/jb.95.3.824-832.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  202. Larsson A., Reichard P. Enzymatic synthesis of deoxyribonucleotides. IX. Allosteric effects in the reduction of pyrimidine ribonucleotides by the ribonucleoside diphosphate reductase system of Escherichia coli. J Biol Chem. 1966 Jun 10;241(11):2533–2539. [PubMed] [Google Scholar]
  203. Larsson A., Reichard P. Enzymatic synthesis of deoxyribonucleotides. X. Reduction of purine ribonucleotides; allosteric behavior and substrate specificity of the enzyme system from Escherichia coli B. J Biol Chem. 1966 Jun 10;241(11):2540–2549. [PubMed] [Google Scholar]
  204. Levitzki A., Koshland D. E., Jr Negative cooperativity in regulatory enzymes. Proc Natl Acad Sci U S A. 1969 Apr;62(4):1121–1128. doi: 10.1073/pnas.62.4.1121. [DOI] [PMC free article] [PubMed] [Google Scholar]
  205. Liebl V., Kaplan J. G., Kushner D. J. Regulation of a salt-dependent enzyme: the aspartate transcarbamylase of an extreme halophile. Can J Biochem. 1969 Dec;47(12):1095–1097. doi: 10.1139/o69-175. [DOI] [PubMed] [Google Scholar]
  206. Lomax M. I., Greenberg G. R. An exchange between the hydrogen atom on carbon 5 of deoxyuridylate and water catalyzed by thymidylate synthetase. J Biol Chem. 1967 Mar 25;242(6):1302–1306. [PubMed] [Google Scholar]
  207. Lomax M. S., Greenberg G. R. Characteristics of the deo operon: role in thymine utilization and sensitivity to deoxyribonucleosides. J Bacteriol. 1968 Aug;96(2):501–514. doi: 10.1128/jb.96.2.501-514.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  208. Long C. W., Levitzki A., Koshland D. E., Jr The subunit structure and subunit interactions of cytidine triphosphate synthetase. J Biol Chem. 1970 Jan 10;245(1):80–87. [PubMed] [Google Scholar]
  209. Lou M. F., Herrmann R. L. A pyrimidine-specific carbamate kinase in Neurospora. Biochim Biophys Acta. 1967 May 16;139(1):199–201. doi: 10.1016/0005-2744(67)90134-9. [DOI] [PubMed] [Google Scholar]
  210. Lue P. F., Kaplan J. G. Heat-induced disaggregation of a multifunctional enzyme complex catalyzing the first steps in pyrimidine biosynthesis in bakers' yeast. Can J Biochem. 1970 Feb;48(2):155–159. doi: 10.1139/o70-024. [DOI] [PubMed] [Google Scholar]
  211. Lue P. F., Kaplan J. G. The aspartate transcarbamylase and carbamoyl phosphate synthetase of yeast: a multi-functional enzyme complex. Biochem Biophys Res Commun. 1969 Feb 21;34(4):426–433. doi: 10.1016/0006-291x(69)90399-4. [DOI] [PubMed] [Google Scholar]
  212. LéJohn H. B., Jackson S. Allosteric interactions of a regulatory nicotinamide adenine dinucleotide-specific glutamate dehydrogenase from Blastocladiella. A molecular model for the enzyme. J Biol Chem. 1968 Jun 25;243(12):3447–3457. [PubMed] [Google Scholar]
  213. MACNUTT W. S. The enzymically catalysed transfer of the deoxyribosyl group from one purine or pyrimidine to another. Biochem J. 1952 Jan;50(3):384–397. doi: 10.1042/bj0500384. [DOI] [PMC free article] [PubMed] [Google Scholar]
  214. MANSON L. A., LAMPEN J. O. The metabolism of desoxyribose nucleosides in Escherichia coli. J Biol Chem. 1951 Dec;193(2):539–547. [PubMed] [Google Scholar]
  215. MARSH J. C., KING M. E. Purification of trans-N-glycosidase of Thermobacter acidophilus: inhibition of enzyme by 6-azathymidine. Biochem Pharmacol. 1959 Aug;2:146–153. doi: 10.1016/0006-2952(59)90081-4. [DOI] [PubMed] [Google Scholar]
  216. MASSEY V., VEEGER C. Studies on the reaction mechanism of lipoyl dehydrogenase. Biochim Biophys Acta. 1961 Mar 18;48:33–47. doi: 10.1016/0006-3002(61)90512-1. [DOI] [PubMed] [Google Scholar]
  217. MICHELSON A. M., DRELL W., MITCHELL H. K. A new ribose nucleoside from Neurospora; "orotidine". Proc Natl Acad Sci U S A. 1951 Jul;37(7):396–399. doi: 10.1073/pnas.37.7.396. [DOI] [PMC free article] [PubMed] [Google Scholar]
  218. MILLER R. W., MASSEY V. DIHYDROOROTIC DEHYDROGENASE. I. SOME PROPERTIES OF THE ENZYME. J Biol Chem. 1965 Mar;240:1453–1465. [PubMed] [Google Scholar]
  219. MONOD J., CHANGEUX J. P., JACOB F. Allosteric proteins and cellular control systems. J Mol Biol. 1963 Apr;6:306–329. doi: 10.1016/s0022-2836(63)80091-1. [DOI] [PubMed] [Google Scholar]
  220. MOORE A. M., BOYLEN J. B. Utilization of uracil by a strain of Escherichia coli. Arch Biochem Biophys. 1955 Feb;54(2):312–317. doi: 10.1016/0003-9861(55)90042-4. [DOI] [PubMed] [Google Scholar]
  221. MOORE E. C., REICHARD P., THELANDER L. ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES.V. PURIFICATION AND PROPERTIES OF THIOREDOXIN REDUCTASE FROM ESCHERICHIA COLI B. J Biol Chem. 1964 Oct;239:3445–3452. [PubMed] [Google Scholar]
  222. Maley G. F., Maley F. The significance of the substrate specificity of T2r+-induced deoxycytidylate deaminase. J Biol Chem. 1966 May 10;241(9):2176–2177. [PubMed] [Google Scholar]
  223. Massey V., Williams C. H., Jr On the reaction mechanism of yeast glutathione reductase. J Biol Chem. 1965 Nov;240(11):4470–4480. [PubMed] [Google Scholar]
  224. Miller R. W., Kerr C. T. Particulate dihydroorotate oxidase system from a pseudomonad. Linkage with the respiratory chain. Can J Biochem. 1967 Sep;45(9):1283–1294. doi: 10.1139/o67-150. [DOI] [PubMed] [Google Scholar]
  225. Molloy A., Finch L. R. Uridine-5'-monophosphate pyrophosphorylase activity from Escherichia coli. FEBS Lett. 1969 Nov 12;5(3):211–213. doi: 10.1016/0014-5793(69)80334-0. [DOI] [PubMed] [Google Scholar]
  226. Munch-Petersen A. On the catabolism of deoxyribonucleosides in cells and cell extracts of Escherichia coli. Eur J Biochem. 1968 Nov;6(3):432–442. doi: 10.1111/j.1432-1033.1968.tb00465.x. [DOI] [PubMed] [Google Scholar]
  227. Munch-Petersen A. Thymidine breakdown and thymine uptake in different mutants of Escherichia coli. Biochim Biophys Acta. 1967 Jun 20;142(1):228–237. doi: 10.1016/0005-2787(67)90530-8. [DOI] [PubMed] [Google Scholar]
  228. Munch-Petersen A. Thymineless mutants of Escherichia coli with deficiencies in deoxyribomutase and deoxyriboaldolase. Biochim Biophys Acta. 1968 Jun 18;161(1):279–282. doi: 10.1016/0005-2787(68)90325-0. [DOI] [PubMed] [Google Scholar]
  229. NEUMANN J., JONES M. E. END-PRODUCT INHIBITION OF ASPARTATE TRANSCARBAMYLASE IN VARIOUS SPECIES. Arch Biochem Biophys. 1964 Mar;104:438–447. doi: 10.1016/0003-9861(64)90487-4. [DOI] [PubMed] [Google Scholar]
  230. Nakanishi S., Ito K., Tatibana M. Two types of carbamyl phosphate synthetase in rat liver: chromatographic resolution and immunological distinction. Biochem Biophys Res Commun. 1968 Dec 9;33(5):774–781. doi: 10.1016/0006-291x(68)90227-1. [DOI] [PubMed] [Google Scholar]
  231. Neuhard J., Ingraham J. Mutants of Salmonella typhimurium requiring cytidine for growth. J Bacteriol. 1968 Jun;95(6):2431–2433. doi: 10.1128/jb.95.6.2431-2433.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  232. Neuhard J., Munch-Petersen A. Studies on the acid-soluble nucleotide pool in thymine-requiring mutants of Escherichia coli during thymine starvation. II. Changes in the amounts of deoxycytidine triphosphate and deoxyadenosine triphosphate in Escherichia coli 15 T-A-U. Biochim Biophys Acta. 1966 Jan 18;114(1):61–71. doi: 10.1016/0005-2787(66)90253-x. [DOI] [PubMed] [Google Scholar]
  233. Neuhard J. Pyrimidine nucleotide metabolism and pathways of thymidine triphosphate biosynthesis in Salmonella typhimurium. J Bacteriol. 1968 Nov;96(5):1519–1527. doi: 10.1128/jb.96.5.1519-1527.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  234. Neuhard J. Studies on the acid-soluble nucleotide pool in Escherichia coli. IV. Effects of hydroxyurea. Biochim Biophys Acta. 1967 Aug 22;145(1):1–6. doi: 10.1016/0005-2787(67)90647-8. [DOI] [PubMed] [Google Scholar]
  235. Neuhard J. Studies on the acid-soluble nucleotide pool in thymine-requiring mutants of Escherichia coli during thymine starvation. 3. On the regulation of the deoxyadenosine triphosphate and deoxycytidine triphosphate pools of Escherichia coli. Biochim Biophys Acta. 1966 Oct 24;129(1):104–115. doi: 10.1016/0005-2787(66)90012-8. [DOI] [PubMed] [Google Scholar]
  236. Nierlich D. P. Amino acid control over RNA synthesis: a re-evaluation. Proc Natl Acad Sci U S A. 1968 Aug;60(4):1345–1352. doi: 10.1073/pnas.60.4.1345. [DOI] [PMC free article] [PubMed] [Google Scholar]
  237. Nikaido H. Biosynthesis of cell wall lipopolysaccharide in gram-negative enteric bacteria. Adv Enzymol Relat Areas Mol Biol. 1968;31:77–124. doi: 10.1002/9780470122761.ch3. [DOI] [PubMed] [Google Scholar]
  238. O'Donovan G. A., Ingraham J. L. Cold-sensitive mutants of Escherichia coli resulting from increased feedback inhibition. Proc Natl Acad Sci U S A. 1965 Aug;54(2):451–457. doi: 10.1073/pnas.54.2.451. [DOI] [PMC free article] [PubMed] [Google Scholar]
  239. O'Donovan G. A. Nucleotide pool changes in mutants of Escherichia coli. Biochim Biophys Acta. 1970;209(2):589–591. doi: 10.1016/0005-2787(70)90761-6. [DOI] [PubMed] [Google Scholar]
  240. O'donovan G. A., Kearney C. L., Ingraham J. L. Mutants of Escherichia coli with High Minimal Temperatures of Growth. J Bacteriol. 1965 Sep;90(3):611–616. doi: 10.1128/jb.90.3.611-616.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  241. OKADA T., HOMMA J., SONOHARA H. Improved method for obtaining thymineless mutants of Escherichia coli and Salmonella typhimurium. J Bacteriol. 1962 Sep;84:602–603. doi: 10.1128/jb.84.3.602-603.1962. [DOI] [PMC free article] [PubMed] [Google Scholar]
  242. OKADA T., YANAGISAWA K., RYAN F. J. A method for securing thymineless mutants from strains of E. coli. Z Vererbungsl. 1961;92:403–412. doi: 10.1007/BF00890061. [DOI] [PubMed] [Google Scholar]
  243. OKAZAKI R., KORNBERG A. DEOXYTHYMIDINE KINASE OF ESCHERICHIA COLI. I. PURIFICATION AND SOME PROPERTIES OF THE ENZYME. J Biol Chem. 1964 Jan;239:269–274. [PubMed] [Google Scholar]
  244. OKAZAKI R., KORNBERG A. DEOXYTHYMIDINE KINASE OF ESCHERICHIA COLI. II. KINETICS AND FEEDBACK CONTROL. J Biol Chem. 1964 Jan;239:275–284. [PubMed] [Google Scholar]
  245. Okada T. Mutational Site of the Gene Controlling Quantitative Thymine Requirement in ESCHERICHIA COLI K-12. Genetics. 1966 Dec;54(6):1329–1336. doi: 10.1093/genetics/54.6.1329. [DOI] [PMC free article] [PubMed] [Google Scholar]
  246. Orengo A. Regulation of enzymic activity by metabolites. I. Uridine-cytidine kinase of Novikoff ascites rat tumor. J Biol Chem. 1969 Apr 25;244(8):2204–2209. [PubMed] [Google Scholar]
  247. Orr M. D., Vitols E. Thioredoxin from Lactobacillus leichmannii and its role as hydrogen donor for ribonucleoside triphosphate reductase. Biochem Biophys Res Commun. 1966 Oct 5;25(1):109–115. doi: 10.1016/0006-291x(66)90647-4. [DOI] [PubMed] [Google Scholar]
  248. Osborn M. J. Structure and biosynthesis of the bacterial cell wall. Annu Rev Biochem. 1969;38:501–538. doi: 10.1146/annurev.bi.38.070169.002441. [DOI] [PubMed] [Google Scholar]
  249. PAEGE L. M., SCHLENK F. Bacterial uracil riboside phosphorylase. Arch Biochem Biophys. 1952 Sep;40(1):42–49. doi: 10.1016/0003-9861(52)90071-4. [DOI] [PubMed] [Google Scholar]
  250. PAEGE L. M., SCHLENK F. Pyrimidine riboside metabolism. Arch Biochem. 1950 Oct;28(3):348–358. [PubMed] [Google Scholar]
  251. PARDEE A. B., YATES R. A. Control of pyrimidine biosynthesis in Escherichia coli by a feed-back mechanism. J Biol Chem. 1956 Aug;221(2):757–770. [PubMed] [Google Scholar]
  252. PARDEE A. B., YATES R. A. Pyrimidine biosynthesis in Escherichia coli. J Biol Chem. 1956 Aug;221(2):743–756. [PubMed] [Google Scholar]
  253. PASTERNAK C. A., HANDSCHUMACHER R. E. The biochemical activity of 6-azauridine: interference with pyrimidine metabolism in transplantable mouse tumors. J Biol Chem. 1959 Nov;234:2992–2997. [PubMed] [Google Scholar]
  254. PASTORE E. J., FRIEDKIN M. The enzymatic synthesis of thymidylate. II. Transfer of tritium from tetrahydrofolate to the methyl group of thymidylate. J Biol Chem. 1962 Dec;237:3802–3810. [PubMed] [Google Scholar]
  255. PRUSOFF W. H. Studies on the mechanism of action of 6-azathymine. I. Biosynthesis of the deoxyriboside. J Biol Chem. 1955 Aug;215(2):809–821. [PubMed] [Google Scholar]
  256. PRUSOFF W. H. Studies on the mechanism of action of azathymine. III. Relationship between incorporation into deoxypentose nucleic acid and inhibition. J Biol Chem. 1957 Jun;226(2):901–910. [PubMed] [Google Scholar]
  257. PRUSOFF W. H., WELCH A. D. Studies on the mechanism of action 6-azathymine. II. Azathymine deoxyriboside, a microbial inhibitor. J Biol Chem. 1956 Feb;218(2):929–939. [PubMed] [Google Scholar]
  258. Paulus H., Gray E. Multivalent feedback inhibition of aspartokinase in Bacillus polymyxa. I. Kinetic studies. J Biol Chem. 1967 Nov 10;242(21):4980–4986. [PubMed] [Google Scholar]
  259. Peterson R. N., Boniface J., Koch A. L. Energy requirements, interactions and distinctions in the mechanisms for transport of various nucleosides in Escherichia coli. Biochim Biophys Acta. 1967 Sep 9;135(4):771–783. doi: 10.1016/0005-2736(67)90108-3. [DOI] [PubMed] [Google Scholar]
  260. Pinsky L., Krooth R. S. Studies on the control of pyrimidine biosynthesis in human diploid cell strains, I. Effect of 6-azauridine on cellular phenotype. Proc Natl Acad Sci U S A. 1967 Apr;57(4):925–932. doi: 10.1073/pnas.57.4.925. [DOI] [PMC free article] [PubMed] [Google Scholar]
  261. Pinsky L., Krooth R. S. Studies on the control of pyrimidine biosynthesis in human diploid cell strains. II. Effects of 5-azaorotic acid, barbituric acid, and pyrimidine precursors on cellular phenotype. Proc Natl Acad Sci U S A. 1967 May;57(5):1267–1274. doi: 10.1073/pnas.57.5.1267. [DOI] [PMC free article] [PubMed] [Google Scholar]
  262. Piérard A. Control of the activity of Escherichia coli carbamoyl phosphate synthetase by antagonistic allosteric effectors. Science. 1966 Dec 23;154(3756):1572–1573. doi: 10.1126/science.154.3756.1572. [DOI] [PubMed] [Google Scholar]
  263. Piérard A., Glansdorff N., Mergeay M., Wiame J. M. Control of the biosynthesis of carbamoyl phosphate in Escherichia coli. J Mol Biol. 1965 Nov;14(1):23–36. doi: 10.1016/s0022-2836(65)80226-1. [DOI] [PubMed] [Google Scholar]
  264. Piérard A., Wiame J. M. Regulation and mutation affecting a glutamine dependent formation of carbamyl phosphate in Escherichia coli. Biochem Biophys Res Commun. 1964 Feb 18;15(1):76–81. doi: 10.1016/0006-291x(64)90106-8. [DOI] [PubMed] [Google Scholar]
  265. Porter R. W., Modebe M. O., Stark G. R. Aspartate transcarbamylase. Kinetic studies of the catalytic subunit. J Biol Chem. 1969 Apr 10;244(7):1846–1859. [PubMed] [Google Scholar]
  266. RACHMELER M., GERHART J., ROSNER J. Limited thymidine uptake in Escherichia coli due to an inducible thymidine phosphorylase. Biochim Biophys Acta. 1961 Apr 29;49:222–225. doi: 10.1016/0006-3002(61)90888-5. [DOI] [PubMed] [Google Scholar]
  267. RACKER E. Enzymatic synthesis and breakdown of desoxyribose phosphate. J Biol Chem. 1952 May;196(1):347–365. [PubMed] [Google Scholar]
  268. RATLIFF R. L., WEAVER R. H., LARDY H. A., KUBY S. A. NUCLEOSIDE TRIPHOSPHATE-NUCLEOSIDE DIPHOSPHATE TRANSPHOSPHORYLASE (NUCLEOSIDE DIPHOSPHOKINASE). I. ISOLATION OF THE CRYSTALLINE ENZYME FROM BREWERS' YEAST. J Biol Chem. 1964 Jan;239:301–309. [PubMed] [Google Scholar]
  269. RAZZELL W. E., CASSHYAP P. SUBSTRATE SPECIFICITY AND INDUCTION OF THYMIDINE PHOSPHORYLASE IN ESCHERICHIA COLI. J Biol Chem. 1964 Jun;239:1789–1793. [PubMed] [Google Scholar]
  270. RAZZELL W. E., KHORANA H. G. Purification and properties of a pyrimidine deoxyriboside phosphorylase from Escherichia coli. Biochim Biophys Acta. 1958 Jun;28(3):562–566. doi: 10.1016/0006-3002(58)90519-5. [DOI] [PubMed] [Google Scholar]
  271. REICHARD P., SKOLD O., KLEIN G. Possible enzymic mechanism for the development of resistance against fluorouracil in ascites tumours. Nature. 1959 Apr 4;183(4666):939–941. doi: 10.1038/183939a0. [DOI] [PubMed] [Google Scholar]
  272. REISSIG J. L. Spectrum of forward mutants in the pyr-3 region of Neurospora. J Gen Microbiol. 1963 Feb;30:327–337. doi: 10.1099/00221287-30-2-327. [DOI] [PubMed] [Google Scholar]
  273. REYNOLDS E. S., LIEBERMAN I., KORNBERG A. The metabolism of orotic acid in aerobic bacteria. J Bacteriol. 1955 Mar;69(3):250–255. doi: 10.1128/jb.69.3.250-255.1955. [DOI] [PMC free article] [PubMed] [Google Scholar]
  274. ROSE I. A., SCHWEIGERT B. S. Incorporation of C14 totally labeled nucleosides into nucleic acids. J Biol Chem. 1953 Jun;202(2):635–645. [PubMed] [Google Scholar]
  275. ROUSH A. H., BETZ R. F. Purification and properties of trans-N-deoxyribosylase. J Biol Chem. 1958 Aug;233(2):261–266. [PubMed] [Google Scholar]
  276. Radford A. Information from ICR-170-induced mutations on the structure of the pyrimidine-3 locus in Neurospora. Mutat Res. 1969 Nov-Dec;8(3):537–544. doi: 10.1016/0027-5107(69)90071-2. [DOI] [PubMed] [Google Scholar]
  277. Radford A. Polarised complementation at the pyrimidine-3 locus of Neurospora. Mol Gen Genet. 1969 Jul 3;104(3):288–294. doi: 10.1007/BF02539292. [DOI] [PubMed] [Google Scholar]
  278. Reichard P. 4th FEBS Meeting's Plenary Lecture. The biosynthesis of deoxyribonucleotides. Eur J Biochem. 1968 Jan;3(3):259–266. doi: 10.1111/j.1432-1033.1968.tb19525.x. [DOI] [PubMed] [Google Scholar]
  279. Reyes P., Heidelberger C. Fluorinated pyrimidines. XXVI. Mammalian thymidylate synthetase: its mechanism of action and inhibition by fluorinated nucleotides. Mol Pharmacol. 1965 Jul;1(1):14–30. [PubMed] [Google Scholar]
  280. Roepke R. R., Mercer F. E. Lethal and Sublethal Effects of X-Rays on Escherichia coli as Related to the Yield of Biochemical Mutants. J Bacteriol. 1947 Dec;54(6):731–743. doi: 10.1128/jb.54.6.731-743.1947. [DOI] [PMC free article] [PubMed] [Google Scholar]
  281. Roepke R. R. Relation between different thymineless mutants derived from Escherichia coli. J Bacteriol. 1967 Mar;93(3):1188–1189. doi: 10.1128/jb.93.3.1188-1189.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  282. SHEPPARD D. E. MUTANTS OF SALMONELLA TYPHIMURIUM RESISTANT TO FEEDBACK INHIBITION BY L-HISTIDINE. Genetics. 1964 Oct;50:611–623. doi: 10.1093/genetics/50.4.611. [DOI] [PMC free article] [PubMed] [Google Scholar]
  283. SIMINOVITCH L., GRAHAM A. F. Synthesis of nucleic acids in Escherichia coli. Can J Microbiol. 1955 Dec;1(9):721–732. doi: 10.1139/m55-086. [DOI] [PubMed] [Google Scholar]
  284. SKODA J., SORM F. Accumulation of nucleic acid metabolites in Escherichia coli exposed to the action of 6-azauracil. Biochim Biophys Acta. 1958 Jun;28(3):659–660. doi: 10.1016/0006-3002(58)90544-4. [DOI] [PubMed] [Google Scholar]
  285. SOMERVILLE R. L., YANOFSKY C. STUDIES ON THE REGULATION OF TRYPTOPHAN BIOSYNTHESIS IN ESCHERICHIA COLI. J Mol Biol. 1965 Apr;11:747–759. doi: 10.1016/s0022-2836(65)80032-8. [DOI] [PubMed] [Google Scholar]
  286. STACEY K. A., SIMSON E. IMPROVED METHOD FOR THE ISOLATION OF THYMINE-REQUIRING MUTANTS OF ESCHERICHIA COLI. J Bacteriol. 1965 Aug;90:554–555. doi: 10.1128/jb.90.2.554-555.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  287. SUYAMA Y., MUNKRES K. D., WOODWARD V. W. Genetic analyses of the pyr-3 locus of Neurospora crassa: the bearing of recombination and gene conversion upon intraallelic linearity. Genetica. 1959;30:293–311. doi: 10.1007/BF01535681. [DOI] [PubMed] [Google Scholar]
  288. Sander E. G., Wright L. D., McCormick D. B. Evidence for function of a metal ion in the activity of dihydroorotase from Zymobacterium oroticum. J Biol Chem. 1965 Sep;240(9):3628–3630. [PubMed] [Google Scholar]
  289. Sanderson K. E. Current linkage map of Salmonella typhimurium. Bacteriol Rev. 1970 Jun;34(2):176–193. doi: 10.1128/br.34.2.176-193.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  290. Saunders P. P., Wilson B. A., Saunders G. F. Purification and comparative properties of a pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus. J Biol Chem. 1969 Jul 10;244(13):3691–3697. [PubMed] [Google Scholar]
  291. Scarano E., Geraci G., Rossi M. Deoxycytidylate aminohydrolase. II. Kinetic properties. The activatory effect of deoxycytidine triphosphate and the inhibitory effect of deoxythymidine triphosphate. Biochemistry. 1967 Jan;6(1):192–201. doi: 10.1021/bi00853a031. [DOI] [PubMed] [Google Scholar]
  292. Schmidt P. G., Stark G. R., Baldeschwieler J. D. Aspartate transcarbamylase. A nuclear magnetic resonance study of the binding of inhibitors and substrates to the catalytic subunit. J Biol Chem. 1969 Apr 10;244(7):1860–1868. [PubMed] [Google Scholar]
  293. Scocca J. J., Panny S. R., Bessman M. J. Studies of deoxycytidylate deaminase from T4-infected Escherichia coli. J Biol Chem. 1969 Jul 10;244(13):3698–3706. [PubMed] [Google Scholar]
  294. Shaffer P. M., McCroskey R. P., Palmatier R. D., Midgett R. J., Abbott M. T. The cell-free conversion of a deoxyribonucleoside to a ribonucleoside without detachment of the deoxyribose. Biochem Biophys Res Commun. 1968 Dec 9;33(5):806–811. doi: 10.1016/0006-291x(68)90232-5. [DOI] [PubMed] [Google Scholar]
  295. Shih A. Y., Eisenstadt J., Lengyel P. On the relation between ribonucleic acid synthesis and peptide chain initiation in E. coli. Proc Natl Acad Sci U S A. 1966 Nov;56(5):1599–1605. doi: 10.1073/pnas.56.5.1599. [DOI] [PMC free article] [PubMed] [Google Scholar]
  296. Skodová H., Skoda J. Mechanism of overproduction of orotic acid by a mutant of Brevibacterium ammoniagenes. Appl Microbiol. 1969 Jan;17(1):188–189. doi: 10.1128/am.17.1.188-189.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  297. Smith D. W., Hanawalt P. C. Macromolecular synthesis and thymineless death in Mycoplasma laidlawii B. J Bacteriol. 1968 Dec;96(6):2066–2076. doi: 10.1128/jb.96.6.2066-2076.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  298. Stadtman E. R. Allosteric regulation of enzyme activity. Adv Enzymol Relat Areas Mol Biol. 1966;28:41–154. doi: 10.1002/9780470122730.ch2. [DOI] [PubMed] [Google Scholar]
  299. Stanier R. Y. Simultaneous Adaptation: A New Technique for the Study of Metabolic Pathways. J Bacteriol. 1947 Sep;54(3):339–348. doi: 10.1128/jb.54.3.339-348.1947. [DOI] [PMC free article] [PubMed] [Google Scholar]
  300. Stryer L., Holmgren A., Reichard P. Thioredoxin. A localized conformational change accompanying reduction of the protein to the sulfhydryl form. Biochemistry. 1967 Apr;6(4):1016–1020. doi: 10.1021/bi00856a009. [DOI] [PubMed] [Google Scholar]
  301. TAKETA K., POGELL B. M. ALLOSTERIC INHIBITION OF RAT LIVER FRUCTOSE 1,6-DIPHOSPHATASE BY ADENOSINE 5'-MONOPHOSPHATE. J Biol Chem. 1965 Feb;240:651–662. [PubMed] [Google Scholar]
  302. TAYLOR A. L., BECKWITH J. R., PARDEE A. B., AUSTRIAN R., JACOB F. THE CHROMOSOMAL LOCATION OF THE STRUCTURAL GENE FOR OROTIDYLIC ACID PYROPHOSPHORYLASE IN ESCHERICHIA COLI. J Mol Biol. 1964 May;8:771–771. doi: 10.1016/s0022-2836(64)80124-8. [DOI] [PubMed] [Google Scholar]
  303. TAYLOR W. H., NOVELLI G. D. ENZYMES OF THE PYRIMIDINE PATHWAY IN ESCHERICHIA COLI. I. SYNTHESIS BY CELLS AND SPHEROPLASTS. J Bacteriol. 1964 Jul;88:99–104. doi: 10.1128/jb.88.1.99-104.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  304. TAYLOR W. H., TAYLOR M. L. ENZYMES OF THE PYRIMIDINE PATHWAY IN ESCHERICHIA COLI. II. INTRACELLULAR LOCALIZATION AND PROPERTIES OF DIHYDROOROTIC DEHYDROGENASE. J Bacteriol. 1964 Jul;88:105–110. doi: 10.1128/jb.88.1.105-110.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  305. Tatibana M., Ito K. Control of pyrimidine biosynthesis in mammalian tissues. I. Partial purification and characterization of glutamine-utilizing carbamyl phosphate synthetase of mouse spleen and its tissue distribution. J Biol Chem. 1969 Oct 10;244(19):5403–5413. [PubMed] [Google Scholar]
  306. Taylor A. L. Current linkage map of Escherichia coli. Bacteriol Rev. 1970 Jun;34(2):155–175. doi: 10.1128/br.34.2.155-175.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  307. Taylor W. H., Taylor M. L., Eames D. F. Two functionally different dihydroorotic dehydrogenases in bacteria. J Bacteriol. 1966 Jun;91(6):2251–2256. doi: 10.1128/jb.91.6.2251-2256.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  308. Thelander L. Studies on thioredoxin reductase from Escherichia coli B. The relation of structure and function. Eur J Biochem. 1968 Apr;4(3):407–419. doi: 10.1111/j.1432-1033.1968.tb00227.x. [DOI] [PubMed] [Google Scholar]
  309. Thelander L. Thioredoxin reductase. Characterization of a homogenous preparation from Escherichia coli B. J Biol Chem. 1967 Mar 10;242(5):852–859. [PubMed] [Google Scholar]
  310. Tomita F., Takahashi I. A novel enzyme, dCTP deaminase, found in Bacillus subtilis infected with phage PBS I. Biochim Biophys Acta. 1969 Mar 18;179(1):18–27. doi: 10.1016/0005-2787(69)90117-8. [DOI] [PubMed] [Google Scholar]
  311. UDAKA S., VENNESLAND B. Properties of triphosphopyridine nucleotide-linked dihydroorotic dehydrogenase. J Biol Chem. 1962 Jun;237:2018–2024. [PubMed] [Google Scholar]
  312. VOGEL H. J. Aspects of repression in the regulation of enzyme synthesis: pathway-wide control and enzyme-specific response. Cold Spring Harb Symp Quant Biol. 1961;26:163–172. doi: 10.1101/sqb.1961.026.01.021. [DOI] [PubMed] [Google Scholar]
  313. Vitols E., Blakley R. L. Hydrogen-donor specificity of ribonucleoside triphosphate reductase from Lactobacillus leichmannii. Biochem Biophys Res Commun. 1965 Dec 9;21(5):466–472. doi: 10.1016/0006-291x(65)90406-7. [DOI] [PubMed] [Google Scholar]
  314. Vitols E., Brownson C., Gardiner W., Blakley R. L. Cobamides and ribonucleotide reduction. V. A kinetic study of the ribonucleoside triphosphate reductase of Lactobacillus leichmannii. J Biol Chem. 1967 Jul 10;242(13):3035–3041. [PubMed] [Google Scholar]
  315. WACKER A., KIRSCHFELD S., TRAGER L. Die Biosynthese der Desoxyribose bei Bakterien. Z Naturforsch B. 1959 Mar;14B(3):145–150. [PubMed] [Google Scholar]
  316. WAHBA A. J., FRIEDKIN M. The enzymatic synthesis of thymidylate. I. Early steps in the purification of thymidylate synthetase of Escherichia coli. J Biol Chem. 1962 Dec;237:3794–3801. [PubMed] [Google Scholar]
  317. WANG T. P., LAMPEN J. O. The cleavage of adenosine, cytidine, and xanthosine by Lactobacillus pentosus. J Biol Chem. 1951 Sep;192(1):339–347. [PubMed] [Google Scholar]
  318. WANG T. P., SABLE H. Z., LAMPEN J. O. Enzymatic deamination of cytosine nucleosides. J Biol Chem. 1950 May;184(1):17–28. [PubMed] [Google Scholar]
  319. WEED L. L., WILSON D. W. Studies on precursors of pyrimidines of nucleic acid. J Biol Chem. 1954 Mar;207(1):439–442. [PubMed] [Google Scholar]
  320. WEED L. L., WILSON D. W. The incorporation of C14-orotic acid into nucleic acid pyrimidines in vitro. J Biol Chem. 1951 Mar;189(1):435–442. [PubMed] [Google Scholar]
  321. WOODWARD V. W. Complementation and recombination on among PYR-3 heteroalleles of Neurospora crassa. Proc Natl Acad Sci U S A. 1962 Mar 15;48:348–356. doi: 10.1073/pnas.48.3.348. [DOI] [PMC free article] [PubMed] [Google Scholar]
  322. WOODWARD V. W., DAVIS R. H. Co-ordinate changes in complementation, suppression and enzyme phenotypes of a PYR-3 mutant of Neurospora crassa. Heredity (Edinb) 1963 Feb;18:21–25. doi: 10.1038/hdy.1963.2. [DOI] [PubMed] [Google Scholar]
  323. WOODWARD V. W., MUNKRES K. D., SUYAMA Y. Uracil metabolism in Neurospora crassa. Experientia. 1957 Dec 15;13(12):484–486. doi: 10.1007/BF02159410. [DOI] [PubMed] [Google Scholar]
  324. WRIGHT L. D., VALENTIK K. A., SPICER D. S., HUFF J. W., SKEGGS H. R. Orotic acid and related compounds in the nutrition of Lactobacillus bulgaricus 09. Proc Soc Exp Biol Med. 1950 Oct;75(1):293–297. doi: 10.3181/00379727-75-18175. [DOI] [PubMed] [Google Scholar]
  325. Wachsman J. T., Kemp S., Kogg L. Thymineless death in Bacillus megaterium. J Bacteriol. 1964 May;87(5):1079–1086. doi: 10.1128/jb.87.5.1079-1086.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  326. Watanabe M. S., McCroskey R. P., Abbott M. T. The enzymatic conversion of 5-formyluracil to uracil 5-carboxylic acid. J Biol Chem. 1970 Apr 25;245(8):2023–2026. [PubMed] [Google Scholar]
  327. Weber K. New structural model of E. coli aspartate transcarbamylase and the amino-acid sequence of the regulatory polypeptide chain. Nature. 1968 Jun 22;218(5147):1116–1119. doi: 10.1038/2181116a0. [DOI] [PubMed] [Google Scholar]
  328. Weitzman P. D., Wilson I. B. Studies on aspartate transcarbamylase and its allosteric interaction. J Biol Chem. 1966 Dec 10;241(23):5481–5488. [PubMed] [Google Scholar]
  329. Wiley D. C., Lipscomb W. N. Crystallographic determination of symmetry of aspartate transcarbamylase. Nature. 1968 Jun 22;218(5147):1119–1121. doi: 10.1038/2181119a0. [DOI] [PubMed] [Google Scholar]
  330. Williams L. G., Mitchell H. K. Mutants affecting thymidine metabolism in Neurospora crassa. J Bacteriol. 1969 Oct;100(1):383–389. doi: 10.1128/jb.100.1.383-389.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  331. Wilson M. C., Farmer J. L., Rothman F. Thymidylate synthesis and aminopterin resistance in Bacillus subtilis. J Bacteriol. 1966 Jul;92(1):186–196. doi: 10.1128/jb.92.1.186-196.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  332. YATES R. A., PARDEE A. B. Control by uracil of formation of enzymes required for orotate synthesis. J Biol Chem. 1957 Aug;227(2):677–692. [PubMed] [Google Scholar]
  333. Yan Y., Demerec M. Genetic analysis of pyrimidine mutants of Salmonella typhimurium. Genetics. 1965 Sep;52(3):643–651. doi: 10.1093/genetics/52.3.643. [DOI] [PMC free article] [PubMed] [Google Scholar]
  334. Yarus M. Recognition of nucleotide sequences. Annu Rev Biochem. 1969;38:841–880. doi: 10.1146/annurev.bi.38.070169.004205. [DOI] [PubMed] [Google Scholar]
  335. Yeh Y. C., Dubovi E. J., Tessman I. Control of pyrimidine biosynthesis by phage T4: mutants unable to catalyze the reduction of cytidine diphosphate. Virology. 1969 Apr;37(4):615–623. doi: 10.1016/0042-6822(69)90279-7. [DOI] [PubMed] [Google Scholar]
  336. ZIMMERMAN S. B., KORNBERG A. Deoxycytidine di- and triphosphate cleavage by an enzyme formed in bacteriophage-infected Eschrichia coli. J Biol Chem. 1961 May;236:1480–1486. [PubMed] [Google Scholar]
  337. Zanetti G., Williams C. H., Jr Characterization of the active center of thioredoxin reductase. J Biol Chem. 1967 Nov 25;242(22):5232–5236. [PubMed] [Google Scholar]

Articles from Bacteriological Reviews are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES