Reaction: Cleavage of Asn3Gln, His10Leu and Ala14Leu in the insulin B chain, and the bond Z-Gly-ProLeu-Gly-Pro in a small molecule substrate of microbial collagenase
Other names: Trimeresurus metalloendopeptidase II; proteinase H2; H2-proteinase
Comments: A 24 kDa nonhemorrhagic endopeptidase from the venom of the habu snake (Trimeresurus flavoviridis). In peptidase family M12 (astacin family)
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 151125-15-4
References.
1. Takahashi, T. and Ohsaka, A. Purification and characterization of a proteinase in the venom of Trimeresurus flavoviridis. Complete separation of the enzyme from hemorrhagic activity. Biochim. Biophys. Acta 198 (1970) 293-307. [PMID: 4984550]
2. Takeya, H., Arakawa, M., Miyata, T., Iwanaga, S. and Omori-Satoh, T. Primary structure of H2-proteinase, a non-hemorrhagic metalloproteinase, isolated from the venom of the habu snake, Trimeresurus flavoviridis. J. Biochem. (Tokyo) 106 (1989) 151-157. [PMID: 2777746]