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Literature summary extracted from
- Spermosin (2004), Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press, 2, 1567-1569.
No PubMed abstract available
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 3.4.21.99 | stabilized by nonionic detergents (Brij 35, Tween 80 or Triton X-100) at 0.005% | Halocynthia roretzi |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.99 | antipain | - |
Halocynthia roretzi |  |
| 3.4.21.99 | Aprotinin | weak | Halocynthia roretzi | |
| 3.4.21.99 | benzyloxycarbonyl-Val-Pro-Arg-H | - |
Halocynthia roretzi | |
| 3.4.21.99 | dansyl-Val-Pro-Arg-H | - |
Halocynthia roretzi | |
| 3.4.21.99 | diisopropyl fluorophosphate | - |
Halocynthia roretzi | |
| 3.4.21.99 | Hg2+ | 1 mM, strong inhibition | Halocynthia roretzi | |
| 3.4.21.99 | leupeptin | weak | Halocynthia roretzi | |
| 3.4.21.99 | p-aminobenzamidine | - |
Halocynthia roretzi | |
| 3.4.21.99 | peptidyl-Arg-H | - |
Halocynthia roretzi | |
| 3.4.21.99 | phenylmethanesulfonyl fluoride | - |
Halocynthia roretzi | |
| 3.4.21.99 | Soybean trypsin inhibitor | weak | Halocynthia roretzi | |
| 3.4.21.99 | Val-Pro-Arg-CH2Cl | - |
Halocynthia roretzi | |
| 3.4.21.99 | Zn2+ | 1 mM, strong inhibition | Halocynthia roretzi | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.21.99 | 0.145 | - |
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarin 7-amide | pH 8.0 | Halocynthia roretzi | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.99 | Ca2+ | 1-10 mM, activates | Halocynthia roretzi | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.99 | 33000 | - |
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 |
| 3.4.21.99 | 40000 | - |
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)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.99 | additional information | Halocynthia roretzi | the enzyme plays an essential role in fertilization of Halocynthia roretzi | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.99 | Halocynthia roretzi | - |
- |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.4.21.99 | proteolytic modification | spermosin is synthesized as a preproenzyme with a molecular mass of 42000 Da, consisting of 388 amino acid residues. The N-terminal 22 residues of preprospermosin correspond to a signal peptide. 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 |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.21.99 | - |
Halocynthia roretzi |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.21.99 | spermatozoon | head region. Partially released from sperm in response to sperm activation or sperm reaction. The enzyme is expressed in the gonad from about half a month before and during the spawning season | Halocynthia roretzi | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.99 | additional information | the enzyme plays an essential role in fertilization of Halocynthia roretzi | Halocynthia roretzi | ? | - |
? | |
| 3.4.21.99 | additional information | the enzyme preferentially or specifically splits the Val-Pro-/-Arg bond in synthetic fluorogenic substrates. The enzyme prefers the Pro residue to Leu, Ser and Gly in the P2 position and prefers the Val residue to Leu, Phe and Gly in the p3 position | Halocynthia roretzi | ? | - |
? | |
| 3.4.21.99 | tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarin 7-amide + H2O | - |
Halocynthia roretzi | tert-butyloxycarbonyl-Val-Pro + Arg-4-methylcoumarin-7-amide | - |
? | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.99 | 8.5 | 9 | - |
Halocynthia roretzi |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 3.4.21.99 | Halocynthia roretzi | - |
- |
6.5 |
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Release 2023.1 (January 2023)
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