Biodegradative l-Threonine Deaminase of Salmonella typhimurium
AUTOR(ES)
Luginbuhl, Geraldine H.
RESUMO
The threonine deaminase formed under anaerobic conditions by Salmonella typhimurium is induced by l-serine and l-threonine, is catabolite repressible, requires cyclic adenosine 3′,5′-monophosphate for its synthesis and adenylic acid for optimal activity, and is immunologically different from biosynthetic threonine deaminase.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=245803Documentos Relacionados
- Synthesis of Branched-Chain Aminoacyl-Transfer Ribonucleic Acid Synthetases in a Salmonella typhimurium Mutant with an Altered Biosynthetic l-Threonine Deaminase
- THREONINE DEAMINATION IN ESCHERICHIA COLI I. : d- and l-Threonine Deaminase Activities of Cell-Free Extracts1
- THREONINE SYNTHASE, A SYSTEM SYNTHESIZING l-THREONINE FROM l-HOMOSERINE1
- Kinetic and Functional Analysis of l-Threonine Kinase, the PduX Enzyme of Salmonella enterica*
- Production of l-Threonine by Auxotrophic Mutants of Escherichia coli