Document Detail


High-efficiency transpeptidation catalysed by clostripain and electrostatic effects in substrate specificity.
MedLine Citation:
PMID:  2327965     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Clostripain catalyses the transpeptidation between benzoylarginin ethyl ester and amino acid amides, oligopeptides, insulin A- and B-chains and tryptic peptides of myoglobin at millimolar substrate concentrations. The reactions proceed with temporary accumulation of the products, followed by hydrolytic decomposition. The yield was not affected significantly by the type of N-terminal amino acid, but was diminished markedly by the negative charges of the amine components. The yields for natural peptides were linearly related to the charge density of the peptides.
Authors:
S Yagisawa; S Watanabe; T Takaoka; H Azuma
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Biochemical journal     Volume:  266     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1990 Mar 
Date Detail:
Created Date:  1990-05-14     Completed Date:  1990-05-14     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  771-5     Citation Subset:  IM    
Affiliation:
Faculty of Pharmaceutical Sciences, Nagasaki University, Japan.
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MeSH Terms
Descriptor/Qualifier:
Acyltransferases / metabolism*
Amino Acid Sequence
Animals
Antibodies, Monoclonal
Chemical Phenomena
Chemistry
Chromatography, High Pressure Liquid
Cysteine Endopeptidases / metabolism*
Horses
Kinetics
Molecular Sequence Data
Peptides
Peptidyl Transferases / metabolism*
Substrate Specificity
Chemical
Reg. No./Substance:
0/Antibodies, Monoclonal; 0/Peptides; EC 2.3.-/Acyltransferases; EC 2.3.2.12/Peptidyl Transferases; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.22.8/clostripain
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