Activation of prothrombin by two subtilisin-like serine proteases from Acremonium sp.

作者：Liu Chunli; Matsushita Yasuhiko; Shimizu Kosuke; Makimura Koichi; Hasumi Keiji^*

来源：Biochemical and Biophysical Research Communications, 2007, 358(1): 356-362.

DOI：10.1016/j.bbrc.2007.04.133

• subtilase
• subtilisin-like serine protease
• prothrombin
• meizothrombin(desF1)
• blood coagulation
• hemostasis

Two novel subtilisin-like serine proteases (AS-E1 and -E2) that activate prothrombin have been identified in a culture of the fungus Acremonium sp. The enzymes were purified through repeated hydrophobic interaction chromatography. The N-terminal sequences of AS-E1 (34.4 kDa) and AS-E2 (32 kDa) showed high similarity to the internal sequences of two distinct subtilisin-like hypothetical proteins from Chaetomium globosum. Both enzymes proteolytically activated prothrombin to meizothrombin(desF1)-like molecules, while the activation cleavage seemed to occur at a site (Tyr(316)-Ile(317)) that is four residues proximal to the canonical Xa cleavage site (Arg(320)-Ile(321)). Both enzymes inhibited plasma clotting, possibly due to extensive degradation of fibrinogen and production of meizothrombin(desF1)-like molecule.

• 出版日期2007-6-22
• 单位河北医科大学