| Gene Cloning and Characterization of α-Amino Acid Ester Acyl Transferase in Empedobacter brevis ATCC14234 and Sphingobacterium siyangensis AJ2458. | |
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MedLine Citation:
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PMID: 22056425 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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The gene encoding α-amino acid ester acyl transferase (AET), the enzyme that catalyzes the peptide-forming reaction from amino acid methyl esters and amino acids, was cloned from Empedobacter brevis ATCC14234 and Sphingobacterium siyangensis AJ2458 and expressed in Escherichia coli. This is the first report on the aet gene. It encodes a polypeptide composed of 616 (ATCC14234) and 619 (AJ2458) amino acids residues. The V(max) values of these recombinant enzymes during the catalysis of L-alanyl-L-glutamine formation from L-alanine methylester and L-glutamine were 1,010 U/mg (ATCC14234) and 1,154 U/mg (AJ2458). An amino acid sequence similarity search revealed 35% (ATCC14234) and 36% (AJ2458) identity with an α-amino acid ester hydrolase from Acetobacter pasteurianus, which contains an active-site serine in the consensus serine enzyme motif, GxSYxG. In the deduced amino acid sequences of AET from both bacteria, the GxSYxG motif was conserved, suggesting that AET is a serine enzyme. |
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Authors:
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Isao Abe; Seiichi Hara; Kenzo Yokozeki |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-11-7 |
Journal Detail:
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Title: Bioscience, biotechnology, and biochemistry Volume: - ISSN: 1347-6947 ISO Abbreviation: - Publication Date: 2011 Nov |
Date Detail:
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Created Date: 2011-11-7 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9205717 Medline TA: Biosci Biotechnol Biochem Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Research Institute for Bioscience Products and Fine Chemicals, Ajinomoto Co., Inc. |
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