Trimerelysin II

Shun ichiro Kawabata, Sadaaki Iwanaga

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

This chapter elaborates the structural chemistry and the biological aspects of trimerelysin II. Four hemorrhagic metalloproteases named HR1A, HR1B, HR2a and HR2b, and one nonhemorrhagic metalloprotease, named H2-proteinase, have been purified from the venom of Trimeresurus flavoviridis. The nonhemorrhagic H2-proteinase protease is assigned the name trimerelysin II. Trimerelysin II is very similar to the hemorrhagic protein HR2a in properties such as molecular mass, pH and heat stability, and susceptibility to EDTA, but it is completely free from a hemorrhagic activity. Trimerelysin II is a nonglycosylated metalloproteinase consisting of 201 amino acid residues with an N-terminal pyroglutamic acid. It contains the typical zinc-binding sequence HEXXH and shows sequence similarity to HR2a. HR2a is also blocked by N-terminal pyroglutamate and consists of 202 residues. It also has 62% identity to the N-terminal protease domain (residues 1–203) of trimerelysin I. HR2a causes hemorrhaging but trimerelysin II does not. The difference may be because of a middle portion of the sequences (residues 51–130 in trimerelysin II) that is only 54% identical between the two proteins and contains a free Cys in trimerelysin II.

Original languageEnglish
Title of host publicationHandbook of Proteolytic Enzymes, Second Edition
Subtitle of host publicationVolume 1: Aspartic and Metallo Peptidases
PublisherElsevier
Pages704-705
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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