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http://purl.uniprot.org/citations/12107130http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12107130http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12107130http://www.w3.org/2000/01/rdf-schema#comment"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 of the forward and reverse reactions are 7 and 9 s(-1), respectively. The K(m) for AEP is 1.11 +/-0.03 mM; for pyruvate it is 0.15 +/- 0.02 mM, for P-Ald it is 0.09 +/-0.01 mM, and for L-Ala it is 1.4 +/-0.03 mM. Substrate specificity tests revealed a high degree of discrimination, indicating a singular physiological role for the transaminase in AEP degradation. The 40-kDa subunit of the homodimeric enzyme is homologous to other members of the pyridoxalphosphate-dependent amino acid transaminase superfamily. Catalytic residues conserved within well-characterized members are also conserved within the seven known AEPT sequences. Site-directed mutagenesis demonstrated the importance of three selected residues (Asp168, Lys194, and Arg340) in AEPT catalysis."xsd:string
http://purl.uniprot.org/citations/12107130http://purl.org/dc/terms/identifier"doi:10.1128/jb.184.15.4134-4140.2002"xsd:string
http://purl.uniprot.org/citations/12107130http://purl.org/dc/terms/identifier"doi:10.1128/jb.184.15.4134-4140.2002"xsd:string
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/author"Martin B.M."xsd:string
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/author"Martin B.M."xsd:string
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/author"Metcalf W.W."xsd:string
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/author"Metcalf W.W."xsd:string
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/author"Dunaway-Mariano D."xsd:string
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/author"Dunaway-Mariano D."xsd:string
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/author"Wanner B.L."xsd:string
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/author"Wanner B.L."xsd:string
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/author"Kim A.D."xsd:string
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/author"Kim A.D."xsd:string
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/author"Baker A.S."xsd:string
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/author"Baker A.S."xsd:string
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/pages"4134-4140"xsd:string
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/pages"4134-4140"xsd:string
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/title"The 2-aminoethylphosphonate-specific transaminase of the 2-aminoethylphosphonate degradation pathway."xsd:string
http://purl.uniprot.org/citations/12107130http://purl.uniprot.org/core/title"The 2-aminoethylphosphonate-specific transaminase of the 2-aminoethylphosphonate degradation pathway."xsd:string