Russellysin

Shun ichiro Kawabata, Sadaaki Iwanaga

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Citation (Scopus)

Abstract

This chapter covers the structural chemistry and the biological aspects of russellysin. Russell's viper venom contains two well-known proteases: a serine protease designated Russell's viper venom factor V activator and a metalloprotease named Russell's viper venom coagulation factor X-activating enzyme (RVV-X). This latter enzyme, known more simply as russellysin, specifically activates coagulation factor X as a result of a single cleavage at the Arg–Ile bond, the same point cleaved by coagulation factors IXa and VIIa. Russellysin is composed of three disulfide-linked chains, a heavy chain of 59 kDa, and two light chains of 18 kDa and 21 kDa. Russellysin is purified from the venom of Daboia (formerly Vipera) russelli. The middle region of the russellysin heavy chain (residues 212–301) shows high sequence similarity to the RGD sequence-containing disintegrins, such as bitistatin (60% identity), trigramin (59% identity), barbourin (55% identity) and echistatin (38% identity). Russellysin is able to inhibit platelet aggregation but the RGD sequence is replaced by Arg-Asp-Glu in the corresponding region. This is similar to the case of Trimeresurus protease HR1B, which has a Glu-Ser-Glu replacement.

Original languageEnglish
Title of host publicationHandbook of Proteolytic Enzymes, Second Edition
Subtitle of host publicationVolume 1: Aspartic and Metallo Peptidases
PublisherElsevier
Pages683-684
Number of pages2
Volume1
ISBN (Electronic)9780120796113
ISBN (Print)9780124121058
DOIs
Publication statusPublished - Jan 1 2004

All Science Journal Classification (ASJC) codes

  • General Biochemistry,Genetics and Molecular Biology

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