Catalytic sites of medicinal leech enzyme destabilase-lysozyme (mlDL): Structure-function relationship |
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Authors: | L L Zavalova N V Antipova Yu I Fadeeva M S Pavlyukov N V Pletneva V Z Pletnev I P Baskova |
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Institution: | 1.Institute of Bioorganic Chemistry,Russian Academy of Sciences,Moscow,Russia;2.Faculty of Biology,Moscow State University,Moscow,Russia |
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Abstract: | Based on the three-dimensional model of the bifunctional enzyme destabilase-lysozyme of the medicinal leech (mlDL) in complex
with trimer of N-acetylglucosamine (NAG)3 by site-directed mutagenesis method, the functional role of the group of amino acids (Glu14, Asp26, Ser29, Ser31, Lys38,
His92) in manifestation of lysozyme (glycosidase, muramidase) and isopeptidase activities has been investigated by site-directed
mutagenesis. The results obtained go well with hypothesis, that lysozyme active site of mlDL includes catalytic Glu14 and
Asp26 residues, and isopeptidase site functions as Ser/Lys catalytic dyad presented by catalytic residues Ser29 and Lys38.
Thus, among the invertebrate lysozymes, mlDL presents the first example of a bifunctional enzyme with identified position
of the isopeptidase active site and localization of the corresponding catalytic residues. |
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