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. 1964 Mar;51(3):390–397. doi: 10.1073/pnas.51.3.390

SERINE DEAMINATION BY THE B PROTEIN OF ESCHERICHIA COLI TRYPTOPHAN SYNTHETASE*

Irving P Crawford 1,†, Junetsu Ito 1
PMCID: PMC300083  PMID: 14171449

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Selected References

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

  1. CRAWFORD I. P. Identification of the triose phosphate formed in the tryptophan synthetase reaction. Biochim Biophys Acta. 1960 Dec 4;45:405–407. doi: 10.1016/0006-3002(60)91474-8. [DOI] [PubMed] [Google Scholar]
  2. CRAWFORD I. P., JOHNSON L. M. Mutants of Escherichia coli defective in the B protein of tryptophan synthetase. I. Selection and classification. Genetics. 1963 May;48:725–736. doi: 10.1093/genetics/48.5.725. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. HATANAKA M., WHITE E. A., HORIBATA K., CRAWFORD I. P. A study of the catalytic properties of Escherichia coli tryptophan synthetase, a two-component enzyme. Arch Biochem Biophys. 1962 Jun;97:596–606. doi: 10.1016/0003-9861(62)90129-7. [DOI] [PubMed] [Google Scholar]
  4. HENNING U., HELINSKI D. R., CHAO F. C., YANOFSKY C. The A protein of the tryptophan synthetase of Escherichia coli. Purification, crystallization, and composition studies. J Biol Chem. 1962 May;237:1523–1530. [PubMed] [Google Scholar]
  5. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  6. MATSUO Y., GREENBERG D. M. A crystalline enzyme that cleaves homoserine and cystathionine. III. Coenzyme resolution, activators, and inhibitors. J Biol Chem. 1959 Mar;234(3):507–515. [PubMed] [Google Scholar]
  7. METZLER D. E., SNELL E. E. Deamination of serine. II. D-Serine dehydrase, a vitamin B6 enzyme from Escherichia coli. J Biol Chem. 1952 Sep;198(1):363–373. [PubMed] [Google Scholar]
  8. NEWTON W. A., SNELL E. E. CATALYTIC PROPERTIES OF TRYPTOPHANASE, A MULTIFUNCTIONAL PYRIDOXAL PHOSPHATE ENZYME. Proc Natl Acad Sci U S A. 1964 Mar;51:382–389. doi: 10.1073/pnas.51.3.382. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. UMBARGER H. E., BROWN B. Threonine deamination in Escherichia coli. II. Evidence for two L-threonine deaminases. J Bacteriol. 1957 Jan;73(1):105–112. doi: 10.1128/jb.73.1.105-112.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. WOOD W. A., GUNSALUS I. C. Serine and threonine desaminaes of Escherichia coli; activators for a cell-free enzyme. J Biol Chem. 1949 Nov;181(1):171–182. [PubMed] [Google Scholar]
  11. YANOFSKY C. The tryptophan synthetase system. Bacteriol Rev. 1960 Jun;24(2):221–245. doi: 10.1128/br.24.2.221-245.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Yanofsky C., Crawford I. P. THE EFFECTS OF DELETIONS, POINT MUTATIONS, REVERSIONS AND SUPPRESSOR MUTATIONS ON THE TWO COMPONENTS OF THE TRYPTOPHAN SYNTHETASE OF ESCHERICHIA COLI. Proc Natl Acad Sci U S A. 1959 Jul;45(7):1016–1026. doi: 10.1073/pnas.45.7.1016. [DOI] [PMC free article] [PubMed] [Google Scholar]

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