[Catalytic sites of medicinal leech enzyme destabilase-lysozyme (Mldl). Structure-functional correlation].
Based on three-dimensional model of the bifunctional enzyme Destabilase-Lysozyme (mlDL-Ds2) in complex with trimer of N-acetylglucosoamine (NAG)3 the functional role of the stereochemically based group of amino acids (Glu14, Asp26, Ser 29, Ser31, Lys38, His92), in manifestation of glycosidase and isopeptidase activities has been elucidated. By method of site-directed mutagenesis it has been shown that mlDL glycosidase active site includes catalytic Glu14 and Asp26, and isopeptidase site functions as Ser/Lys dyad presented by catalytic residues Lys38 and Ser29. Thus, among the invertebrate lysozymes mlDL presents first example of the bifunctional enzyme with identified position of the isopeptidase active site and localization of the corresponding catalytic residues.
L L
LL
Zavalova
N V
NV
Antipova
Iu I
IuI
Fadeeva
M S
MS
Pavliukov
N V
NV
Pletneva
V Z
VZ
Pletnev
I P
IP
Baskova
D019943:Amino Acid Substitution; D000818:Animals; D020134:Catalytic Domain; D010450:Endopeptidases / Q000737:chemistry* / Q000235:genetics; D047709:Hirudo medicinalis / Q000201:enzymology* / Q000235:genetics; D016297:Mutagenesis, Site-Directed; D020125:Mutation, Missense; D013329:Structure-Activity Relationship
D010450:Endopeptidases; C045348:fibrin destabilase