Trimerelysin I

Shun ichiro Kawabata, Sadaaki Iwanaga

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

This chapter presents an overview of the structural chemistry and the biological aspects of trimerelysin I. In the 1970s, four hemorrhagic metalloproteinases, HR1A, HR1B, HR2a and HR2b, and one nonhemorrhagic proteinase, H2-proteinase, were purified from the venom of the habu snake, Trimeresurus flavoviridis. HR1A has been designated trimerelysin I by IUBMB; the related HR1B has not yet been classified. Studies on the substrate specificity of these venom metalloproteinases, using the oxidized insulin B chain, show that they both have an identical primary specificity, favoring bulky hydrophobic residues such as Leu and Met at P1. No structural studies have been performed on HRIA (trimerelysin I). HRIB is a mosaic protein composed of 416 amino acid residues containing four Asn-linked oligosaccharide chains, and the N-terminal half (residues 1–203) contains a metalloproteinase domain with sequence similarity to HR2a (62% identity) and atrolysin C (52% identity). HRIA and HRIB are purified from the venom of Trimeresurus flavoviridis.

Original languageEnglish
Title of host publicationHandbook of Proteolytic Enzymes, Second Edition
Subtitle of host publicationVolume 1: Aspartic and Metallo Peptidases
PublisherElsevier
Pages702-703
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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