Biology:Trimerelysin II
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Trimerelysin II | |||||||||
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Identifiers | |||||||||
EC number | 3.4.24.53 | ||||||||
CAS number | 151125-15-4 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Trimerelysin II (EC 3.4.24.53, Trimeresurus metalloendopeptidase II, proteinase H2, H2-proteinase) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Cleavage of Asn3-Gln, His10-Leu and Ala14-Leu in the insulin B chain, and the bond Z-Gly-Pro-Leu-Gly-Pro in a small molecule substrate of microbial collagenase
This endopeptidase is present in the venom of the habu snake (Trimeresurus flavoviridis).
References
- ↑ "Purification and characterization of a proteinase in the venom of Trimeresurus flavoviridis. Complete separation of the enzyme from hemorrhagic activity". Biochimica et Biophysica Acta (BBA) - Enzymology 198 (2): 293–307. February 1970. doi:10.1016/0005-2744(70)90062-8. PMID 4984550.
- ↑ "Primary structure of H2-proteinase, a non-hemorrhagic metalloproteinase, isolated from the venom of the habu snake, Trimeresurus flavoviridis". Journal of Biochemistry 106 (1): 151–7. July 1989. doi:10.1093/oxfordjournals.jbchem.a122805. PMID 2777746.
External links
- Trimerelysin+II at the US National Library of Medicine Medical Subject Headings (MeSH)
Original source: https://en.wikipedia.org/wiki/Trimerelysin II.
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