| Specificity for various imino-acid-residues of a proline-specific dipeptidylcarboxypeptidase from a Streptomyces species. | |
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MedLine Citation:
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PMID: 8448197 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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A proline-specific dipeptidylcarboxypeptidase, which removes diproline from the C-terminus of the proline-containing peptides, such as Boc-Pro-Pro-Pro-Pro and Leu-Pro-Pro-Pro-Pro-Pro, has recently been purified from a Streptomyces sp. The specificity of the enzyme for various imino acid-containing synthetic peptide substrates was further studied. The peptides with proline, hydroxyproline, or dehydroproline at the P2' position were found to be good substrates, while those with pipecolic acid, D-proline or other usual amino acids at the P2' position were scarcely hydrolyzed. The peptides with proline, dehydroproline, pipecolic acid, or N-methyl-alanine at the P1' position were well-hydrolyzed, while those with hydroxyproline or D-proline at the P1' position were not hydrolyzed. Utilizing this high specificity for imino acids, Boc-Pro-Pro-Pro-Pro was synthesized by the enzyme using Boc-Pro-Pro as the acidic component and Pro-Pro as the basic component. |
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Authors:
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S Maruyama; S Miyoshi; G Nomura; M Suzuki; H Tanaka; H Maeda |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 1162 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 1993 Mar |
Date Detail:
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Created Date: 1993-04-13 Completed Date: 1993-04-13 Revised Date: 2004-11-17 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 72-6 Citation Subset: IM |
Affiliation:
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Fermentation Research Institute, Agency of Industrial Science and Technology, Ibaraki, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Carboxypeptidases / isolation & purification, metabolism* Endopeptidases / isolation & purification, metabolism* Hydrolysis Imino Acids / metabolism* Molecular Sequence Data Peptide Biosynthesis Peptides / metabolism Proline / metabolism* Stereoisomerism Streptomyces / enzymology* Substrate Specificity |
| Chemical | |
Reg. No./Substance:
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0/Imino Acids; 0/Peptides; 147-85-3/Proline; EC 3.4.-/Carboxypeptidases; EC 3.4.-/Endopeptidases; EC 3.4.15.-/proline-specific dipeptidylcarboxypeptidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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