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J Bacteriol. 1971 June; 106(3): 972-982
Copyright © 1971 American Society for Microbiology. All Rights Reserved.

Biochemical Bases for the Antimetabolite Action of L-Serine Hydroxamate

Tetsuya Tosa1 and Lewis I. Pizer

a Department of Microbiology, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104

ABSTRACT

The amino acid analogue L-serine hydroxamate, which is bacteriostatic for Escherichia coli, has been shown to inhibit protein synthesis. The antimetabolite is a competitive inhibitor of seryl-transfer ribonucleic acid (tRNA) synthetase with a Ki value of 30 µM. Mutants resistant to L-serine hydroxamate have been selected, and three were shown to have seryl-tRNA synthetases with increased Ki values. One mutant contains a 3-phosphoglycerate dehydrogenase which is insensitive to inhibition by L-serine.


FOOTNOTES

1 Present address: Chemical Research Laboratory, Tanabe Seiyaku Co., Ltd., Osaka, Japan.


J Bacteriol. 1971 June; 106(3): 972-982
Copyright © 1971 American Society for Microbiology. All Rights Reserved.




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