Spermosin
| Spermosin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.21.99 | ||||||||
| CAS number | 89925-67-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Spermosin (EC 3.4.21.99) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Hydrolyses arginyl bonds, preferably with Pro in the P2 position
This enzyme is isolated from the ascidian (Prochordate) Halocynthia roretzi.
References
- ↑ Sawada, H.; Yokosawa, H.; Ishii, S. (1984). "Purification and characterization of two types of trypsin-like enzymes from sperm of the ascidian (Prochordata) Halocynthia roretzi. Evidence for the presence of spermosin, a novel acrosin-like enzyme". J. Biol. Chem. 259: 2900–2904. PMID 6365918.
- ↑ Sawada, H.; Yokosawa, H.; Someno, T.; Saino, T.; Ishii, S. (1984). "Evidence for the participation of two sperm proteases, spermosin and acrosin, in fertilization of the ascidian, Halocynthia roretzi: inhibitory effects of leupeptin analogs on enzyme activities and fertilization". Dev. Biol. 105: 246–249. doi:10.1016/0012-1606(84)90281-1. PMID 6381175.
- ↑ Sawada, H.; Iwasaki, K.; Kihara-Negishi, F.; Ariga, H.; Yokosawa, H. (1996). "Localization, expression, and the role in fertilization of spermosin, an ascidian sperm trypsin-like protease". Biochem. Biophys. Res. Commun. 222: 499–504. doi:10.1006/bbrc.1996.0773. PMID 8670234.
- ↑ Sawada, H.; Someno, T. (1996). "Substrate specificity of ascidian sperm trypsin-like proteases, spermosin and acrosin". Mol. Reprod. Dev. 45: 240–243. doi:10.1002/(SICI)1098-2795(199610)45:2<240::AID-MRD18>3.0.CO;2-4. PMID 8914083.
External links
- Spermosin at the US National Library of Medicine Medical Subject Headings (MeSH)
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