|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 18.104.22.168
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Mass balance status: Undetermined; a substrate lacks a chemical formula
Enzyme Commission Primary Name: spermosin
Enzyme Commission Summary:
Hydrolyzes arginyl bonds, preferably with Pro in the P2 position.
The enzyme from the ascidian (Prochordate) Halocynthia roretzi is localised in the sperm head, and released during sperm activation.
A proline-rich region is involved in binding to the vitelline coat of the egg.
Belongs to peptidase family S1.
Sawada84: 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(5);2900-4. PMID: 6365918
Sawada84a: 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(1);246-9. PMID: 6381175
Sawada96: 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(2);499-504. PMID: 8670234
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