EC Number |
General Information |
Reference |
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3.4.21.74 | evolution |
the enzyme belongs to the peptidase S1 family, snake venom subfamily |
755600 |
3.4.21.74 | metabolism |
proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview |
755604 |
3.4.21.74 | more |
construction of a three-dimensional model of VaaSPH-1 bound to FVIIIa |
755581 |
3.4.21.74 | more |
determination of 13 surface-located B cell-recognized linear epitopes of a Lachesis stenophrys venom serine proteinase. The corresponding peptides are synthesized and their immunoreactivity is analyzed against a panel of experimental and therapeutic antivenoms. Molecular modeling of the Lachesis stenophrys enzyme using as a template the structure of the Deinagkistrodon acutus Dav-PA serine proteinase (Q9I8X1), which displays the highest degree of sequence similarity to the Lachesis stenophrys enzyme among proteins of known 3D structure, and the surface-located epitopes are identified in the protein model using iCn3D |
755600 |
3.4.21.74 | more |
gloshedobin is a thrombin-like enzyme from the venom of Gloydius shedaoensis |
717128 |
3.4.21.74 | more |
molecular modeling of the Lachesis stenophrys enzyme (Q072L7) using as a template the structure of the Deinagkistrodon acutus Dav-PA serine proteinase (Q9I8X1), which displays the highest degree of sequence similarity to the Lachesis stenophrys enzyme among proteins of known 3D structure, and the surface-located epitopes are identified in the protein model using iCn3D |
755600 |
3.4.21.74 | more |
the catalytic triad comprises residues His42, Asp86, and Ser194, simulation of molecular dynamics, overview |
731423 |
3.4.21.74 | more |
the enzyme is a thrombin-like serine protease |
718430 |
3.4.21.74 | physiological function |
a glycoprotein from the nose-horned viper (Vipera ammodytes ammodytes [Vaa]) venom, Vaa serine proteinase homolog 1 (VaaSPH-1), structurally is a serine protease but without an enzymatic activity. It exhibits potent anticoagulant action in human blood. One of its targets in the blood coagulation system is FVIIIa of the intrinsic tenase complex, where VaaSPH-1 antagonizes the binding of FIXa. VaaSPH-1 also inhibits extrinsic tenase activity |
755581 |
3.4.21.74 | physiological function |
enzyme VaF1 is a high molecular mass metalloproteinase with alpha-fibrinogenolytic activity from nose-horned viper (Vipera ammodytes ammodytes) venom |
752844 |