Ontology highlight
ABSTRACT:
SUBMITTER: Kim AD
PROVIDER: S-EPMC135204 | biostudies-literature | 2002 Aug
REPOSITORIES: biostudies-literature
Kim Alexander D AD Baker Angela S AS Dunaway-Mariano Debra D Metcalf W W WW Wanner B L BL Martin Brian M BM
Journal of bacteriology 20020801 15
The 2-aminoethylphosphonate transaminase (AEPT; the phnW gene product) of the Salmonella enterica serovar Typhimurium 2-aminoethylphosphonate (AEP) degradation pathway catalyzes the reversible reaction of AEP and pyruvate to form phosphonoacetaldehyde (P-Ald) and L-alanine (L-Ala). Here, we describe the purification and characterization of recombinant AEPT. pH rate profiles (log V(m) and log V(m)/K(m) versus pH) revealed a pH optimum of 8.5. At pH 8.5, K(eq) is equal to 0.5 and the k(cat) values ...[more]