Literature summary for 3.4.21.74 extracted from

Latinovic, Z.; Leonardi, A.; Kovacic, L.; Koh, C.; Sribar, J.; Bakija, A.; Venkateswarlu, D.; Kini, R.; Krizaj, I.
The first intrinsic tenase complex inhibitor with serine protease structure offers a new perspective in anticoagulant therapy (2018), Thromb. Haemost., 118, 1713-1728 .

Search for more literature for 3.4.21.74

Application

Application	Comment	Organism
drug development	VaaSPH-1 represents a very promising template to design low molecular mass FVIIIa-directed anticoagulant substances, based on structural features of the interaction surface between VaaSPH-1 and FVIIIa. Construction of a three-dimensional model of VaaSPH-1 bound to FVIIIa. The model exposes the 157-loop and the preceding alpha-helix as the most appropriate structural elements of VaaSPH-1 to be considered as a guideline to synthesize small FVIIIa-binding molecules, potential different generation of anticoagulants	Vipera ammodytes ammodytes
medicine	components of the intrinsic blood coagulation pathway, among them factor VIIIa (FVIIIa), have been recognized as suitable therapeutic targets to treat venous thromboembolism, pathological process behind two very serious cardiovascular diseases, deep vein thrombosis and pulmonary embolism. Enzyme VaaSPH-1 cab be a safe anticoagulant since it lacks proteolytic activity different from the contemporary drugs, which frequently induce excessive bleeding and other complications, during medical application. VaaSPH-1 is unlikely to be orally available for chronic usage as it has molecular mass of 35 kDa	Vipera ammodytes ammodytes

Organism

Organism	UniProt	Comment	Textmining
Vipera ammodytes ammodytes	A0A1I9KNP0	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	binding of enzyme VaaSPH-1 to lipids, overview	Vipera ammodytes ammodytes	?	-	?

Synonyms

Synonyms	Comment	Organism
Vaa serine proteinase homolog 1	-	Vipera ammodytes ammodytes
VaaSPH-1	-	Vipera ammodytes ammodytes

General Information

General Information	Comment	Organism
additional information	construction of a three-dimensional model of VaaSPH-1 bound to FVIIIa	Vipera ammodytes ammodytes
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	Vipera ammodytes ammodytes

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)