Hydroxyamino acid utilization and alpha-ketobutyrate toxicity in Pseudomonas cepacia.
AUTOR(ES)
Wong, H C
RESUMO
Growth of Pseudomonas cepacia 249 on D-threonine required a mutation to permit D-hydroxyamino acid deaminase formation and L-valine to overcome alpha-ketobutyrate toxicity. Strain 249 lacked a second D-hydroxyamino acid deaminase formed by other strains.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=294680Documentos Relacionados
- Substrate channeling: alpha-ketobutyrate inhibition of acetohydroxy acid synthase in Salmonella typhimurium.
- Toxic accumulation of alpha-ketobutyrate caused by inhibition of the branched-chain amino acid biosynthetic enzyme acetolactate synthase in Salmonella typhimurium.
- Enzymes related to fructose utilization in Pseudomonas cepacia.
- Pleiotropic effects of poxA regulatory mutations of Escherichia coli and Salmonella typhimurium, mutations conferring sulfometuron methyl and alpha-ketobutyrate hypersensitivity.
- Pseudomonas cepacia.