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Peculiarities of substrate hydrolysis by endopeptidases from hepatopancreas of king crab

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Abstract

Kinetic parameters of hydrolysis of peptide and protein substrates by psychrophilic endopeptidases from hepatopancreas of the king crab Paralithodes camtschaticus (PC), in particular, by trypsin, collagenolytic protease, and metalloprotease, were measured at different temperatures. The PC trypsin was shown to hydrolyze Bz-Arg-pNA in the temperature range studied (4–37°C) 19 times more effectively than bovine trypsin. The rate constants of hydrolysis of Glp-Ala-Ala-Leu-pNA by the PC collagenolytic protease increased approximately by one order of magnitude along with temperature decrease, while K m decreased by 3.5 times. The effective values of K m for the hydrolysis of azocasein by the metalloprotease insignificantly depend on temperature. We proposed that electrostatic interactions of negative charges around the cavity of active site are critical for the effective hydrolysis of substrates by endopeptidases of the PC hepatopancreas.

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Abbreviations

PC:

Paralithodes camtschaticus

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Authors and Affiliations

  1. Faculty of Chemistry, Moscow State University, Vorob’evy gory, Moscow, 119992, Russia

    A. I. Papisova, S. A. Semenova, Yu. A. Kislitsyn & G. N. Rudenskaya

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  1. A. I. Papisova
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  2. S. A. Semenova
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  3. Yu. A. Kislitsyn
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  4. G. N. Rudenskaya
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Correspondence to G. N. Rudenskaya.

Additional information

This is a publication on the materials of the VI Symposium on the Chemistry of Proteolytic Enzymes; see Russian Journal of Bioorganic Chemistry, 2008, vol. 34, no. 5

Original Russian Text © A.I. Papisova, S.A. Semenova, Yu.A. Kislitsyn, G.N. Rudenskaya, 2008, published in Bioorganicheskaya Khimiya, 2008, Vol. 34, No. 4, pp. 479–486.

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Papisova, A.I., Semenova, S.A., Kislitsyn, Y.A. et al. Peculiarities of substrate hydrolysis by endopeptidases from hepatopancreas of king crab. Russ J Bioorg Chem 34, 428–434 (2008). https://doi.org/10.1134/S1068162008040067

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  • DOI: https://doi.org/10.1134/S1068162008040067

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