Deoxycytidine Triphosphate Deaminase: Characterization of an Escherichia coli Mutant Deficient in the Enzyme-Reference-Cited by-同舟云学术

Deoxycytidine Triphosphate Deaminase: Characterization of an Escherichia coli Mutant Deficient in the Enzyme

Published:1971-02 Issue:2 Volume:105 Page:666-672
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

O'Donovan G. A.¹²,Edlin G.¹²,Fuchs J. A.¹²,Neuhard J.¹²,Thomassen E.¹²

Affiliation:

1. Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843

2. Enzyme Division, University Institute of Biological Chemistry B, Copenhagen K, Denmark

Abstract

A mutant of Escherichia coli , previously shown to contain abnormal nucleoside triphosphate pools, was found to be defective in its ability to synthesize thymidine nucleotides. The defect is not in the enzyme thymidylate synthetase but in deoxycytidine triphosphate deaminase, an enzyme that supplies deoxyuridine monophosphate, the substrate for thymidylate synthetase.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/jb.105.2.666-672.1971

Reference24 articles.

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3. Release of repressor control of ribonucleotide reductase by thymine starvation;Biswas C.;J. Biol. Chem.,1965

4. Mutant bacteria showing efficient utilization of thymidine;Fangman W. L.;J. Bacteriol.,1966

5. Deoxyuridylate kinase activity and deoxyuridine triphosphatase in Escherichia coli;Greenberg G. R.;Proc. Nat. Acad. Sci. U.S.A.,1962

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