Gene cloning and characterization of α-amino acid ester acyl transferase in Empedobacter brevis ATCC14234 and Sphingobacterium siyangensis AJ2458.
作者： Isao ABE , Seiichi HARA , Kenzo YOKOZEKI
DOI: 10.1271/BBB.110181
关键词:
摘要: The gene encoding α-amino acid ester acyl transferase (AET), the enzyme that catalyzes peptide-forming reaction from amino methyl esters and acids, was cloned Empedobacter brevis ATCC14234 Sphingobacterium siyangensis AJ2458 expressed in Escherichia coli. This is first report on aet gene. It encodes a polypeptide composed of 616 (ATCC14234) 619 (AJ2458) acids residues. V(max) values these recombinant enzymes during catalysis L-alanyl-L-glutamine formation L-alanine methylester L-glutamine were 1,010 U/mg 1,154 (AJ2458). An sequence similarity search revealed 35% 36% identity with an hydrolase Acetobacter pasteurianus, which contains active-site serine consensus motif, GxSYxG. In deduced sequences AET both bacteria, GxSYxG motif conserved, suggesting enzyme.
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