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J Bacteriol. 1971 February; 105(2): 666-672
Copyright © 1971 American Society for Microbiology. All Rights Reserved.

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

G. A. O'Donovan, G. Edlin1, J. A. Fuchs, J. Neuhard2 and E. Thomassen2

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


FOOTNOTES

1 Present address: Department of Genetics, University of California, Davis, Calif. 95616.

2 Present address: Department of Bacteriology, University of California, Davis, Calif. 95616.


J Bacteriol. 1971 February; 105(2): 666-672
Copyright © 1971 American Society for Microbiology. All Rights Reserved.




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