beta-Chloro-L-alanine inhibition of the Escherichia coli alanine-valine transaminase.
AUTOR(ES)
Whalen, W A
RESUMO
beta-Chloro-L-alanine, an amino acid analog which inhibits a number of enzymes, reversibly inhibited the Escherichia coli K-12 alanine-valine transaminase, transaminase C. This inhibition, along with the inhibition of transaminase B, accounted for the isoleucine-plus-valine requirement of E. coli in the presence of beta-chloro-L-alanine.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=219336Documentos Relacionados
- Cloning and characterization of the Escherichia coli K-12 alanine-valine transaminase (avtA) gene.
- Role of alanine-valine transaminase in Salmonella typhimurium and analysis of an avtA::Tn5 mutant.
- ISOLEUCINE AND VALINE METABOLISM IN ESCHERICHIA COLI XI. K-12: Valine Inhibition of the Growth of Escherichia coli Strain1
- Beta-alanine synthesis in Escherichia coli.
- Inhibition of Bacterial Growth by β-Chloro-D-Alanine
