Carboxypeptidase from Streptomyces bikiniensis: Primary Structure, Isolation, and Properties

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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, and G. G. Chestukhina

Institute for Genetics and Selection of Industrial Microorganisms, 1-yi Dorozhnyi Proezd 1, 117545 Moscow, Russia; fax: (495) 315-0347; E-mail: ingvarzal@mail.ru; zalunin@genetika.ru

^* To whom correspondence should be addressed.

Received January 22, 2010; Revision received March 22, 2010

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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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KEY WORDS: Streptomyces bikiniensis, metallocarboxypeptidase, substitution therapy

DOI: 10.1134/S0006297910080122

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