Biochemical Bases for the Antimetabolite Action of l-Serine Hydroxamate
AUTOR(ES)
Tosa, Tetsuya
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=248741Documentos Relacionados
- l-Serine Production by a Mutant of Sarcina albida Defective in l-Serine Degradation
- l-Serine Catabolism via an Oxygen-Labile l-Serine Dehydratase Is Essential for Colonization of the Avian Gut by Campylobacter jejuni
- l-Serine Deaminase of Escherichia coli
- Production of L-serine by Sarcina albida.
- Cloning and expression of the two genes coding for L-serine dehydratase from Peptostreptococcus asaccharolyticus: relationship of the iron-sulfur protein to both L-serine dehydratases from Escherichia coli.