Document Detail


A novel l-amino acid ligase from bacillus licheniformis.
MedLine Citation:
PMID:  18930013     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
l-Amino acid alpha-ligase (EC 6.3.2.28) catalyzed formation of alpha-peptide bond in unprotected l-amino acids in an ATP-dependent manner. BL00235 gene in Bacillus licheniformis NBRC12200 coded as a new l-amino acid ligase. BL00235 substrate specificity was strict; only methionine or leucine was acceptable as dipeptide N-terminal residues.
Authors:
Kuniki Kino; Atsushi Noguchi; Yuji Nakazawa; Makoto Yagasaki
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of bioscience and bioengineering     Volume:  106     ISSN:  1347-4421     ISO Abbreviation:  J. Biosci. Bioeng.     Publication Date:  2008 Sep 
Date Detail:
Created Date:  2008-10-20     Completed Date:  2009-01-09     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100888800     Medline TA:  J Biosci Bioeng     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  313-5     Citation Subset:  IM    
Affiliation:
Department of Applied Chemistry, Faculty of Science and Engineering, Waseda University, 3-4-1 Ohkubo, Shinjuku-ku, Tokyo 169-8555, Japan.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacillus / enzymology*
Enzyme Activation
Enzyme Stability
Molecular Sequence Data
Peptide Synthases / chemistry*
Chemical
Reg. No./Substance:
EC 6.3.2.-/Peptide Synthases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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