Document Detail


Substrate specificity of aminopeptidase from the mid-gut gland of the scallop (Patinopecten yessoensis).
MedLine Citation:
PMID:  15118330     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
An action for various peptides and a kinetic study for amino acid p-nitroanilides (pNAs) and 4-methylcoumaryl-7-amides (MCAs) were performed with purified aminopeptidase from the mid-gut of the scallop. The enzyme preferred dipeptides having Ala, Met, and Phe in the amino-terminal or the penultimate position from the amino-termini. The catalytic efficiencies, k(cat)/K(m) values for Ala-pNA and MCA were the highest in the tested substrates, and those for pNA and MCA substrates having Met or Phe were the next highest. The enzyme was found to be a new alanine-specific aminopeptidase.
Authors:
Hironori Umetsu; Mito Arai; Toshinori Ota; Kaoru Abe; Hidemitsu Uchizawa; Kazuo Sasaki
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Bioscience, biotechnology, and biochemistry     Volume:  68     ISSN:  0916-8451     ISO Abbreviation:  Biosci. Biotechnol. Biochem.     Publication Date:  2004 Apr 
Date Detail:
Created Date:  2004-04-30     Completed Date:  2005-01-11     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9205717     Medline TA:  Biosci Biotechnol Biochem     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  945-7     Citation Subset:  IM    
Affiliation:
Graduate School of Environmental Science, Aomori University, Kobata, Japan. umetsu@aomori-u.ac.jp
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MeSH Terms
Descriptor/Qualifier:
Aminopeptidases / metabolism*
Animals
Hydrolysis
Intestines / enzymology*
Kinetics
Mollusca / anatomy & histology*,  enzymology*
Substrate Specificity
Chemical
Reg. No./Substance:
EC 3.4.11.-/Aminopeptidases

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


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