OXAMIC TRANSCARBAMYLASE OF STREPTOCOCCUS ALLANTOICUS-Reference-Cited by-同舟云学术

OXAMIC TRANSCARBAMYLASE OF STREPTOCOCCUS ALLANTOICUS

Published:1964-01 Issue:1 Volume:87 Page:75-80
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Bojanowski R.¹,Gaudy Elizabeth¹,Valentine R. C.¹,Wolfe R. S.¹

Affiliation:

1. Department of Microbiology, University of Illinois, Urbana, Illinois

Abstract

Bojanowski , R. (University of Illinois, Urbana), Elizabeth Gaudy, R. C. Valentine, and R. S. Wolfe . Oxamic transcarbamylase of Streptococcus allantoicus . J. Bacteriol. 87: 75–80. 1964.—An improved colorimetric assay for carbamyl oxamate, which allows the precise measurement of the activity of oxamic transcarbamylase, has been developed. Activity is maximum over the pH range from 8.3 to 8.7. A cation requirement is satisfied by 2.5 × 10 −3 m Mg ++ or Mn ++ . The equilibrium constant for the phosphorolysis of carbamyl oxamic acid is 1.6, corresponding to a negative free energy change of −285 cal per mole.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/jb.87.1.75-80.1964

Reference15 articles.

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4. BOJANOWSKI R. R. C. VALENTINE E. T. GAUDY AND R. S. WOLFE. 1962. Oxamic transcarbamylase. Bacteriol. Proc. p. 103.

5. Synthesis of citrulline with animal and bacterial enzymes;CARAVACA J.;J. Biol. Chem.,1960

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