|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 184.108.40.206
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.
Mass balance status: The left side is missing: Peptides: 2 . The right side is missing: Proteins: 1 O: 1 H: 1
Enzyme Commission Primary Name: spermosin
Taxonomic Range: Metazoa
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): 36.144756 [Latendresse13]
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
©2016 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493