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Spermosin

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Spermosin
Identifiers
EC no.3.4.21.99
CAS no.89925-67-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
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NCBIproteins

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

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  1. ^ Sawada H, Yokosawa H, Ishii S (March 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". The Journal of Biological Chemistry. 259 (5): 2900–4. PMID 6365918.
  2. ^ Sawada H, Yokosawa H, Someno T, Saino T, Ishii S (September 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". Developmental Biology. 105 (1): 246–9. doi:10.1016/0012-1606(84)90281-1. PMID 6381175.
  3. ^ Sawada H, Iwasaki K, Kihara-Negishi F, Ariga H, Yokosawa H (May 1996). "Localization, expression, and the role in fertilization of spermosin, an ascidian sperm trypsin-like protease". Biochemical and Biophysical Research Communications. 222 (2): 499–504. doi:10.1006/bbrc.1996.0773. PMID 8670234.
  4. ^ Sawada H, Someno T (October 1996). "Substrate specificity of ascidian sperm trypsin-like proteases, spermosin and acrosin". Molecular Reproduction and Development. 45 (2): 240–3. doi:10.1002/(SICI)1098-2795(199610)45:2<240::AID-MRD18>3.0.CO;2-4. PMID 8914083.
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