Trimerelysin II
| Trimerelysin II | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.53 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
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
- ^ Takahashi T, Ohsaka A (February 1970). "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. doi:10.1016/0005-2744(70)90062-8. PMID 4984550.
- ^ Takeya H, Arakawa M, Miyata T, Iwanaga S, Omori-Satoh T (July 1989). "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. doi:10.1093/oxfordjournals.jbchem.a122805. PMID 2777746.
External links
- Trimerelysin+II at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
