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Carboxypeptidase from Streptomyces bikiniensis: Primary structure, isolation, and properties

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Abstract

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 and Affiliations

  1. Institute for Genetics and Selection of Industrial Microorganisms, 1-yi Dorozhnyi Proezd 1, 117545, Moscow, Russia

    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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  1. A. V. Serkina
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  2. I. A. Zalunin
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  3. E. I. Levitin
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  4. T. A. Voejkova
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  5. B. V. Tyaglov
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  6. L. M. Novikova
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  7. L. K. Emeljanova
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  8. G. E. Konstantinova
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  9. G. G. Chestukhina
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Correspondence to I. A. Zalunin.

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Original Russian Text © 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, 2010, published in Biokhimiya, 2010, Vol. 75, No. 8, pp. 1142–1149.

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Serkina, A.V., Zalunin, I.A., Levitin, E.I. et al. Carboxypeptidase from Streptomyces bikiniensis: Primary structure, isolation, and properties. Biochemistry Moscow 75, 1032–1038 (2010). https://doi.org/10.1134/S0006297910080122

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  • DOI: https://doi.org/10.1134/S0006297910080122

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