Full text
PDFSelected References
These references are in PubMed. This may not be the complete list of references from this article.
- Ahmad N., Siddiqi M. Bacterial metabolism of 3-hydroxy-3-methylglutaric acid. J Bacteriol. 1973 Jul;115(1):162–167. doi: 10.1128/jb.115.1.162-167.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bannerjee D., Sanders L. E., Sokatch J. R. Properties of purified methylmalonate semialdehyde dehydrogenase of Pseudomonas aeruginosa. J Biol Chem. 1970 Apr 10;245(7):1828–1835. [PubMed] [Google Scholar]
- Bowden J. A., Connelly J. L. Branched chain alpha-keto acid metabolism. II. Evidence for the common identity of alpha-ketoisocaproic acid and alpha-keto-beta-methyl-valeric acid dehydrogenases. J Biol Chem. 1968 Jun 25;243(12):3526–3531. [PubMed] [Google Scholar]
- Calhoun D. H., Hatfield G. W. Autoregulation: a role for a biosynthetic enzyme in the control of gene expression. Proc Natl Acad Sci U S A. 1973 Oct;70(10):2757–2761. doi: 10.1073/pnas.70.10.2757. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Coleman M. S., Armstrong F. B. Branched-chain amino-acid aminotransferase of Salmonella typhimurium. I. Crystallization and preliminary characterization. Biochim Biophys Acta. 1971 Jan 13;227(1):56–66. doi: 10.1016/0005-2744(71)90167-7. [DOI] [PubMed] [Google Scholar]
- Coleman M. S., Soucie W. G., Armstrong F. B. Branched chain amino acid aminotransferase of Salmonella typhimurium. II. Kinetic comparison with the enzyme from Salmonella montevideo. J Biol Chem. 1971 Mar 10;246(5):1310–1312. [PubMed] [Google Scholar]
- Connelly J. L., Danner D. J., Bowden J. A. Branched chain alpha-keto acid metabolism. I. Isolation, purification, and partial characterization of bovine liver alpha-ketoisocaproic:alpha-keto-beta-methylvaleric acid dehydrogenase. J Biol Chem. 1968 Mar 25;243(6):1198–1203. [PubMed] [Google Scholar]
- Conrad R. S., Massey L. K., Sokatch J. R. D- and L-isoleucine metabolism and regulation of their pathways in Pseudomonas putida. J Bacteriol. 1974 Apr;118(1):103–111. doi: 10.1128/jb.118.1.103-111.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Coudert M. Charcterization and physiological function of a soluble L-amino acid oxidase in Corynebacterium. Arch Microbiol. 1975;102(2):151–153. doi: 10.1007/BF00428360. [DOI] [PubMed] [Google Scholar]
- Duerre J. A., Chakrabarty S. l-amino acid oxidases of Proteus rettgeri. J Bacteriol. 1975 Feb;121(2):656–663. doi: 10.1128/jb.121.2.656-663.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Engel P. C., Massey V. The purification and properties of butyryl-coenzyme A dehydrogenase from Peptostreptococcus elsdenii. Biochem J. 1971 Dec;125(3):879–887. doi: 10.1042/bj1250879. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Goodhue C. T., Snell E. E. The bacterial degradation of pantothenic acid. 3. Enzymatic formation of aldopantoic acid. Biochemistry. 1966 Feb;5(2):403–408. doi: 10.1021/bi00866a003. [DOI] [PubMed] [Google Scholar]
- Goodhue C. T., Snell E. E. The bacterial degradation of pantothenic acid. I. Over-all nature of the reaction. Biochemistry. 1966 Feb;5(2):393–398. doi: 10.1021/bi00866a001. [DOI] [PubMed] [Google Scholar]
- HILZ H., KNAPPE J., RINGELMANN E., LYNEN F. Methylglutaconase, eine neue Hydratase, die am Stoffwechsel verzweigter Carbonsäuren beteiligt ist. Biochem Z. 1958;329(6):476–489. [PubMed] [Google Scholar]
- HIMES R. H., YOUNG D. L., RINGELMANN E., LYNEN F. The biochemical function of biotin. V. Further studies on beta-methylcrotonyl CoA carboxylase. Biochem Z. 1963;337:48–61. [PubMed] [Google Scholar]
- Hill F., Schlegel H. G. Die alpha-Isopropylmalat-Synthetase bei Hydrogenomonas H 16. Arch Mikrobiol. 1969;68(1):1–17. doi: 10.1007/BF00408442. [DOI] [PubMed] [Google Scholar]
- Kaneda T. Biosynthesis of branched long-chain fatty acids from the related short-chain -keto acid substrates by a cell-free system of Bacillus subtilis. Can J Microbiol. 1973 Jan;19(1):87–96. doi: 10.1139/m73-013. [DOI] [PubMed] [Google Scholar]
- Kates M. Biosynthesis of lipids in microorganisms. Annu Rev Microbiol. 1966;20:13–44. doi: 10.1146/annurev.mi.20.100166.000305. [DOI] [PubMed] [Google Scholar]
- Kohlhaw G., Leary T. R., Umbarger H. E. Alpha-isopropylmalate synthase from Salmonella typhimurium. Purification and properties. J Biol Chem. 1969 Apr 25;244(8):2218–2225. [PubMed] [Google Scholar]
- Magee P. T., Snell E. E. The bacterial degradation of pantothenic acid. IV. Enzymatic conversion of aldopantoate to alpha-ketoisovalerate. Biochemistry. 1966 Feb;5(2):409–416. doi: 10.1021/bi00866a004. [DOI] [PubMed] [Google Scholar]
- Marinus M. G., Loutit J. S. Regulation of isoleucine-valine biosynthesis in Pseudomonas aeruginosa. I. Characterisation and mapping of mutants. Genetics. 1969 Nov;63(3):547–556. doi: 10.1093/genetics/63.3.547. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Marshall V. D., Sokatch J. R. Regulation of valine catabolism in Pseudomonas putida. J Bacteriol. 1972 Jun;110(3):1073–1081. doi: 10.1128/jb.110.3.1073-1081.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Marshall V. P., Sokatch J. R. Oxidation of D-amino acids by a particulate enzyme from Pseudomonas aeruginosa. J Bacteriol. 1968 Apr;95(4):1419–1424. doi: 10.1128/jb.95.4.1419-1424.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Martin R. R., Marshall V. D., Sokatch J. R., Unger L. Common enzymes of branched-chain amino acid catabolism in Pseudomonas putida. J Bacteriol. 1973 Jul;115(1):198–204. doi: 10.1128/jb.115.1.198-204.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Massey L. K., Conrad R. S., Sokatch J. R. Regulation of leucine catabolism in Pseudomonas putida. J Bacteriol. 1974 Apr;118(1):112–120. doi: 10.1128/jb.118.1.112-120.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mäntsälä P. Product induction in the degradation of pantothenate in Pseudomonas fluorescens P-2. J Gen Microbiol. 1971 Aug;67(2):239–242. doi: 10.1099/00221287-67-2-239. [DOI] [PubMed] [Google Scholar]
- Namba Y., Yoshizawa K., Ejima A., Hayashi T., Kaneda T. Coenzyme A- and nicotinamide adenine dinucleotide-dependent branched chain alpha-keto acid dehydrogenase. I. Purification and properties of the enzyme from Bacillus subtilis. J Biol Chem. 1969 Aug 25;244(16):4437–4447. [PubMed] [Google Scholar]
- Norton J. E., Sokatch J. R. Purification and partial characterization of the branched chain amino acid transaminase of Pseudomonas aeruginosa. Biochim Biophys Acta. 1970 May 13;206(2):261–269. doi: 10.1016/0005-2744(70)90109-9. [DOI] [PubMed] [Google Scholar]
- Norton J. E., Sokath J. R. Oxidation of D- and L-valine by enzymes of Pseudomonas aeruginosa. J Bacteriol. 1966 Jul;92(1):116–120. doi: 10.1128/jb.92.1.116-120.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nurmikko V., Salo E., Hakola H., Mäkinen K., Snell E. E. The bacterial degradation of pantothenic acid. II. Pantothenate hydrolase. Biochemistry. 1966 Feb;5(2):399–402. doi: 10.1021/bi00866a002. [DOI] [PubMed] [Google Scholar]
- Ornston L. N. Regulation of catabolic pathways in Pseudomonas. Bacteriol Rev. 1971 Jun;35(2):87–116. doi: 10.1128/br.35.2.87-116.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pauli G., Overath P. ato Operon: a highly inducible system for acetoacetate and butyrate degradation in Escherichia coli. Eur J Biochem. 1972 Sep 25;29(3):553–562. doi: 10.1111/j.1432-1033.1972.tb02021.x. [DOI] [PubMed] [Google Scholar]
- Puukka M., Laakso S., Nurmikko V. Regulation of valine degradation in Pseudomonas fluorescens UK-1. Induction of methylmalonate semialdehyde dehydrogenase. Acta Chem Scand. 1973;27(2):720–722. doi: 10.3891/acta.chem.scand.27-0720. [DOI] [PubMed] [Google Scholar]
- Puukka M., Lönnberg H., Nurmikko V. Regulation of branched chain amino acid transaminase formation during the growth of Pseudomonas fluorescens UK-1. Acta Chem Scand. 1972;26(3):1271–1273. doi: 10.3891/acta.chem.scand.26-1271. [DOI] [PubMed] [Google Scholar]
- Puukka M., Mäntsälä P., Lönnberg H., Pajula R., Nurmikko V. Formation of 2-oxoisovalerate dehydrogenase in Pseudomonas fluorescens. Acta Chem Scand. 1972;26(3):1299–1301. doi: 10.3891/acta.chem.scand.26-1299. [DOI] [PubMed] [Google Scholar]
- Puukka M. Regulation of valine degradation in Pseudomonas fluorescens UK-1. Induction of enoyl coenzyme A hydratase. Acta Chem Scand. 1973;27(2):718–719. doi: 10.3891/acta.chem.scand.27-0718. [DOI] [PubMed] [Google Scholar]
- RILLING H. C., COON M. J. The enzymatic isomerization of alpha-methylvinylacetyl coenzyme A and the specificity of a bacterial alpha-methylcrotonyl coenzyme A carboxylase. J Biol Chem. 1960 Nov;235:3087–3092. [PubMed] [Google Scholar]
- ROBINSON W. G., COON M. J. The purification and properties of beta-hydroxyisobutyric dehydrogenase. J Biol Chem. 1957 Mar;225(1):511–521. [PubMed] [Google Scholar]
- RUDMAN D., MEISTER A. Transamination in Escherichia coli. J Biol Chem. 1953 Feb;200(2):591–604. [PubMed] [Google Scholar]
- Rheinwald J. G., Chakrabarty A. M., Gunsalus I. C. A transmissible plasmid controlling camphor oxidation in Pseudomonas putida. Proc Natl Acad Sci U S A. 1973 Mar;70(3):885–889. doi: 10.1073/pnas.70.3.885. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rüdiger H. W., Langenbeck U., Goedde H. W. Oxidation of branched chain -ketoacids in Streptococcus faecalis and it's dependence on lipoic acid. Hoppe Seylers Z Physiol Chem. 1972 Jun;353(6):875–882. doi: 10.1515/bchm2.1972.353.1.875. [DOI] [PubMed] [Google Scholar]
- SASAKI S. On the decarboxylase operating in the degradative pathway of L-leucine by Proteus vulgaris. J Biochem. 1962 May;51:335–344. [PubMed] [Google Scholar]
- SEUBERT W., FASS E. UNTERSUCHUNGEN UEBER DEN BAKTERIELLEN ABBAU VO ISOPRENOIDEN. IV. REINIGUNG UND EIGENSCHAFTEN DER BETA-ISOHEXENYLGLUTACONYL-COA-HYDRATASE UND BETA-HYDROXY-BETA-ISOHEXENYLGLUTARYL-COA-LYASE. Biochem Z. 1964 Dec 7;341:23–34. [PubMed] [Google Scholar]
- SEUBERT W., FASS E. UNTERSUCHUNGEN UEBER DEN BAKTERIELLEN ABBAU VON ISOPRENOIDEN. V. DER MECHANISMUS DES ISOPRENOIDABBAUES. Biochem Z. 1964 Dec 7;341:35–44. [PubMed] [Google Scholar]
- Sala-Trepat J. M., Murray K., Williams P. A. The metabolic divergence in the meta cleavage of catechols by Pseudomonas putida NCIB 10015. Physiological significance and evolutionary implications. Eur J Biochem. 1972 Jul 24;28(3):347–356. doi: 10.1111/j.1432-1033.1972.tb01920.x. [DOI] [PubMed] [Google Scholar]
- Siddiqi M. A., Rodwell V. W. Bacterial metabolism of mevalonic acid. J Bacteriol. 1967 Jan;93(1):207–214. doi: 10.1128/jb.93.1.207-214.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sokatch J. R., Sanders L. E., Marshall V. P. Oxidation of methylmalonate semialdehyde to propionyl coenzyme A in Pseudomonas aeruginosa grown on valine. J Biol Chem. 1968 May 25;243(10):2500–2506. [PubMed] [Google Scholar]
- Stanier R. Y., Palleroni N. J., Doudoroff M. The aerobic pseudomonads: a taxonomic study. J Gen Microbiol. 1966 May;43(2):159–271. doi: 10.1099/00221287-43-2-159. [DOI] [PubMed] [Google Scholar]
- Tsukada K. D-amino acid dehydrogenases of Pseudomonas fluorescens. J Biol Chem. 1966 Oct 10;241(19):4522–4528. [PubMed] [Google Scholar]
- Voellmy R., Leisinger T. Dual role for N-2-acetylornithine 5-aminotransferase from Pseudomonas aeruginosa in arginine biosynthesis and arginine catabolism. J Bacteriol. 1975 Jun;122(3):799–809. doi: 10.1128/jb.122.3.799-809.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Waterson R. M., Castellino F. J., Hass G. M., Hill R. L. Purification and characterization of crotonase from Clostridium acetobutylicum. J Biol Chem. 1972 Aug 25;247(16):5266–5271. [PubMed] [Google Scholar]
- Weeks G., Shapiro M., Burns R. O., Wakil S. J. Control of fatty acid metabolism. I. Induction of the enzymes of fatty acid oxidation in Escherichia coli. J Bacteriol. 1969 Feb;97(2):827–836. doi: 10.1128/jb.97.2.827-836.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Willecke K., Pardee A. B. Fatty acid-requiring mutant of bacillus subtilis defective in branched chain alpha-keto acid dehydrogenase. J Biol Chem. 1971 Sep 10;246(17):5264–5272. [PubMed] [Google Scholar]
- Winnacker E. L., Barker H. A. Aerobic metabolism of -amino-n-butyric acid by Pseudomonas putida. Biochim Biophys Acta. 1971 May 18;237(2):284–292. doi: 10.1016/0304-4165(71)90319-9. [DOI] [PubMed] [Google Scholar]
- YONEYA T., ADAMS E. Hydroxyproline metabolism. V. Inducible allohydroxy-D-proline oxidase of Pseudomonas. J Biol Chem. 1961 Dec;236:3272–3279. [PubMed] [Google Scholar]