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PMID: 4934072 Published · ppublish English Journal Article

Biochemical bases for the antimetabolite action of L-serine hydroxamate.

Journal of bacteriology ·Vol. 106 ·No. 3 ·1971-06-00 ·Pages 972-82

Tosa T, Pizer LI

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 mum. 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.

MeSH Terms
Bacterial Proteins/biosynthesis Carbon Isotopes Culture Media Drug Resistance, Microbial Escherichia coli/drug effects,enzymology,growth & development,metabolism Genetics, Microbial Glycerolphosphate Dehydrogenase/metabolism Glycine/metabolism Hydroxamic Acids/pharmacology Leucine/metabolism Ligases/antagonists & inhibitors,metabolism Mutagens Mutation Nitrosoguanidines RNA, Bacterial/biosynthesis Serine/metabolism,pharmacology Spectrophotometry Stereoisomerism Threonine/metabolism Tritium Ultracentrifugation Uracil/metabolism
Chemicals
Bacterial Proteins Carbon Isotopes Culture Media Hydroxamic Acids Mutagens Nitrosoguanidines RNA, Bacterial Tritium Threonine Serine Uracil Glycerolphosphate Dehydrogenase Ligases Leucine Glycine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Tosa T
Pizer L I
References (18)
18 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1971-06-00
Pages
972-82
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC248741
Subset
IM
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