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 K i value of 30 μ m . Mutants resistant to l -serine hydroxamate have been selected, and three were shown to have seryl-tRNA synthetases with increased K i values. One mutant contains a 3-phosphoglycerate dehydrogenase which is insensitive to inhibition by l -serine.
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Dates
Type | When |
---|---|
Created | 5 years, 7 months ago (Jan. 3, 2020, 9:31 a.m.) |
Deposited | 4 years, 1 month ago (July 29, 2021, 12:58 p.m.) |
Indexed | 3 weeks, 2 days ago (Aug. 7, 2025, 5:09 a.m.) |
Issued | 54 years, 2 months ago (June 1, 1971) |
Published | 54 years, 2 months ago (June 1, 1971) |
Published Print | 54 years, 2 months ago (June 1, 1971) |
@article{Tosa_1971, title={Biochemical Bases for the Antimetabolite Action of <scp>l</scp> -Serine Hydroxamate}, volume={106}, ISSN={1098-5530}, url={http://dx.doi.org/10.1128/jb.106.3.972-982.1971}, DOI={10.1128/jb.106.3.972-982.1971}, number={3}, journal={Journal of Bacteriology}, publisher={American Society for Microbiology}, author={Tosa, Tetsuya and Pizer, Lewis I.}, year={1971}, month=jun, pages={972–982} }