| Substrate specificity of aminopeptidase from the mid-gut gland of the scallop (Patinopecten yessoensis). | |
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MedLine Citation:
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PMID: 15118330 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Hironori Umetsu; Mito Arai; Toshinori Ota; Kaoru Abe; Hidemitsu Uchizawa; Kazuo Sasaki |
Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Bioscience, biotechnology, and biochemistry Volume: 68 ISSN: 0916-8451 ISO Abbreviation: Biosci. Biotechnol. Biochem. Publication Date: 2004 Apr |
Date Detail:
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Created Date: 2004-04-30 Completed Date: 2005-01-11 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 9205717 Medline TA: Biosci Biotechnol Biochem Country: Japan |
Other Details:
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Languages: eng Pagination: 945-7 Citation Subset: IM |
Affiliation:
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Graduate School of Environmental Science, Aomori University, Kobata, Japan. umetsu@aomori-u.ac.jp |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Aminopeptidases
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metabolism* Animals Hydrolysis Intestines / enzymology* Kinetics Mollusca / anatomy & histology*, enzymology* Substrate Specificity |
| Chemical | |
Reg. No./Substance:
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EC 3.4.11.-/Aminopeptidases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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