From Wikipedia, the free encyclopedia
Spermosin
Identifiers
EC no. 3.4.21.99
CAS no. 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
Search
PMC articles
PubMed articles
NCBI proteins

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

  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.
From Wikipedia, the free encyclopedia
Spermosin
Identifiers
EC no. 3.4.21.99
CAS no. 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
Search
PMC articles
PubMed articles
NCBI proteins

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

  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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