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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