Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1960 Apr;75(1):3–12. doi: 10.1042/bj0750003

The synthesis of methionine from homocysteine by enzymic extracts of Escherichia coli

J Szulmajster 1, D D Woods 1
PMCID: PMC1204320  PMID: 13836466

Full text

PDF
3

Selected References

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

  1. ARNSTEIN H. R., NEUBERGER A. The effect of cobalamin on the quantitative utilization of serine, glycine and formate for the synthesis of choline and methyl groups of methionine. Biochem J. 1953 Sep;55(2):259–271. doi: 10.1042/bj0550259. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. CROSS M. J., WOODS D. D. The synthesis of methionine by cell-free extracts of Bacterium coli. Biochem J. 1954 Jul 16;58(331ST):xvi–xvii. [PubMed] [Google Scholar]
  3. EMERSON S. Competitive reactions and antagonisms in the biosynthesis of amino acids by neurospora. Cold Spring Harb Symp Quant Biol. 1950;14:40–48. doi: 10.1101/sqb.1950.014.01.007. [DOI] [PubMed] [Google Scholar]
  4. GIBSON F., WOODS D. D. The synthesis of methionine by suspensions of Escherichia coli. Biochem J. 1960 Jan;74:160–172. doi: 10.1042/bj0740160. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. GIBSON F., WOODS D. D. The synthesis of methionine from homocysteine by Escherichia coli. Biochem J. 1952 Apr;51(1):v–v. [PubMed] [Google Scholar]
  6. KISLIUK R. L., SAKAMI W. A study of the mechanism of serine biosynthesis. J Biol Chem. 1955 May;214(1):47–57. [PubMed] [Google Scholar]
  7. KUBY S. A., NODA L., LARDY H. A. Adenosinetriphosphate-creatine transphosphorylase. III. Kinetic studies. J Biol Chem. 1954 Sep;210(1):65–82. [PubMed] [Google Scholar]
  8. LASCELLES J., CROSS M. J., WOODS D. D. The folic acid and serine nutrition of Leuconostoc mesenteroides P60 (Streptococcus equinus P60). J Gen Microbiol. 1954 Apr;10(2):267–284. doi: 10.1099/00221287-10-2-267. [DOI] [PubMed] [Google Scholar]
  9. NAKAO A., GREENBERG D. M. Studies on the incorporation of isotope from formaldehyde-C14 and serine-3-C14 into the methyl group of methionine. J Biol Chem. 1958 Feb;230(2):603–620. [PubMed] [Google Scholar]
  10. SHOCKMAN G. D., TOENNIES G. Formation of d-methionine from 1-by Streptococcus faecalis. Arch Biochem Biophys. 1954 May;50(1):9–17. doi: 10.1016/0003-9861(54)90003-x. [DOI] [PubMed] [Google Scholar]
  11. STADTMAN E. R., NOVELLI G. D., LIPMANN F. Coenzyme A function in and acetyl transfer by the phosphotransacetylase system. J Biol Chem. 1951 Jul;191(1):365–376. [PubMed] [Google Scholar]
  12. STICKLAND L. H. The determination of small quantities of bacteria by means of the biuret reaction. J Gen Microbiol. 1951 Oct;5(4):698–703. doi: 10.1099/00221287-5-4-698. [DOI] [PubMed] [Google Scholar]
  13. TOENNIES G., SHOCKMAN G. D. Quantitative amino acid assimilation in homofermentative metabolism. Arch Biochem Biophys. 1953 Aug;45(2):447–458. doi: 10.1016/s0003-9861(53)80021-4. [DOI] [PubMed] [Google Scholar]
  14. WRIGHT B. E., STADTMAN T. C. The rôle of polyglutamyl pteridine coenzymes in serine metabolism. I. Cofactor requirements in the conversion of serine to glycine. J Biol Chem. 1956 Apr;219(2):863–871. [PubMed] [Google Scholar]
  15. WRIGHT B. E. The rôle of polyglutamyl pteridine coenzymes in serine metabolism. II. A comparison of various pteridine derivatives. J Biol Chem. 1956 Apr;219(2):873–883. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES