| Carboxypeptidase from Streptomyces bikiniensis: primary structure, isolation, and properties. | |
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MedLine Citation:
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PMID: 21073425 Owner: NLM Status: In-Process |
Abstract/OtherAbstract:
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A metallocarboxypeptidase produced by Streptomyces bikiniensis 27 strain (VKPM Ac-1783) (CPSb) was purified and characterized. The enzyme cleaves both basic and hydrophobic C-terminal amino acid residues from synthetic peptides, that is, it possesses specificity of mammalian carboxypeptidases A and B. The enzyme also hydrolyzes peptides bearing glutamic acid at the C-end. CPSb exhibits its maximal activity at pH 7.0-7.6 and 55°C. The nucleotide sequence encoding the mature CPSb in S. bikiniensis 27 (VKPM Ac-1783) genome (Accession No. GU362077) was determined. It is shown that the primary structure of the mature enzyme has a moderate degree of identity with orthologs from Streptomyces griseus (79% identity) and Streptomyces avermitilis (85% identity). |
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Authors:
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A V Serkina; I A Zalunin; E I Levitin; T A Voejkova; B V Tyaglov; L M Novikova; L K Emeljanova; G E Konstantinova; G G Chestukhina |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Biochemistry. Biokhimii͡a Volume: 75 ISSN: 1608-3040 ISO Abbreviation: Biochemistry Mosc. Publication Date: 2010 Aug |
Date Detail:
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Created Date: 2010-11-15 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0376536 Medline TA: Biochemistry (Mosc) Country: United States |
Other Details:
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Languages: eng Pagination: 1032-8 Citation Subset: IM |
Affiliation:
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Institute for Genetics and Selection of Industrial Microorganisms, Moscow, 117545, Russia. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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