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Literature summary for 3.4.21.99 extracted from

  • Kodama, E.; Baba, T.; Kohno, N.; Satoh, S.; Yokosawa, H.; Sawada, H.
    Spermosin, a trypsin-like protease from ascidian sperm: cDNA cloning, protein structures and functional analysis (2002), Eur. J. Biochem., 269, 657-663.
    View publication on PubMed
Search for more literature for 3.4.21.99

Cloned(Commentary)

Cloned (Comment) Organism
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 Halocynthia roretzi

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
33000
-
 there are two forms of spermosin in the sperm: the 33000 Da spermosin is made up of the heavy chain (residues 130-388) and the light chain (residues 97-129). The 40000 Da enzyme form consists of the heavy chain (residues 130-388) and the light chain (residues 23-129) Halocynthia roretzi
40000
-
 there are two forms of spermosin in the sperm: the 33000 Da spermosin is made up of the heavy chain (residues 130-388) and the light chain (residues 97-129). The 40000 Da enzyme form consists of the heavy chain (residues 130-388) and the light chain (residues 23-129) Halocynthia roretzi

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Halocynthia roretzi the enzyme binds to the vitelline coat plays a key role in sperm penetration through the vitelline coat during ascidian fertilization ?
-
 ?

Organism

Organism UniProt Comment Textmining
Halocynthia roretzi Q966V2
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification preprospermosin has a MW of 41896 Da. The N-terminal sequence of the preprospermosin corresponds to a signal peptide for a nascent protein destined for initial transfer to the endoplasmic reticulum. The pro-form of spermosin may start from Ser23 Halocynthia roretzi

Purification (Commentary)

Purification (Comment) Organism
-
 Halocynthia roretzi

Source Tissue

Source Tissue Comment Organism Textmining
gonad
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 Halocynthia roretzi
-
additional information no activity detected in hepatopancreas, intestine and brachial basket Halocynthia roretzi
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme binds to the vitelline coat plays a key role in sperm penetration through the vitelline coat during ascidian fertilization Halocynthia roretzi ?
-
 ?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarin 7-amide + H2O
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 Halocynthia roretzi tert-butyloxycarbonyl-Val-Pro + Arg-4-methylcoumarin-7-amide
-
 ?