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

Abstract：

: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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Liu C,Matsushita Y,Shimizu K,Makimura K,Hasumi K

doi

10.1016/j.bbrc.2007.04.133

subject

Has Abstract

pub_date

2007-06-22 00:00:00

pages

356-62

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)00878-9

journal_volume

358

pub_type

杂志文章

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