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Literature summary for 3.4.21.99 extracted from

  • Lindsay, L.L.
    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
Search for more literature for 3.4.21.99

General Stability

General Stability Organism
stabilized by nonionic detergents (Brij 35, Tween 80 or Triton X-100) at 0.005% Halocynthia roretzi

Inhibitors

Inhibitors Comment Organism Structure
antipain
-
 Halocynthia roretzi
Aprotinin weak Halocynthia roretzi
benzyloxycarbonyl-Val-Pro-Arg-H
-
 Halocynthia roretzi
dansyl-Val-Pro-Arg-H
-
 Halocynthia roretzi
diisopropyl fluorophosphate
-
 Halocynthia roretzi
Hg2+ 1 mM, strong inhibition Halocynthia roretzi
leupeptin weak Halocynthia roretzi
p-aminobenzamidine
-
 Halocynthia roretzi
peptidyl-Arg-H
-
 Halocynthia roretzi
phenylmethanesulfonyl fluoride
-
 Halocynthia roretzi
Soybean trypsin inhibitor weak Halocynthia roretzi
Val-Pro-Arg-CH2Cl
-
 Halocynthia roretzi
Zn2+ 1 mM, strong inhibition Halocynthia roretzi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.145
-
 tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarin 7-amide pH 8.0 Halocynthia roretzi

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ 1-10 mM, activates Halocynthia roretzi

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Halocynthia roretzi the enzyme plays an essential role in fertilization of Halocynthia roretzi ?
-
 ?

Organism

Organism UniProt Comment Textmining
Halocynthia roretzi
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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)

Purification (Comment) Organism
-
 Halocynthia roretzi

Source Tissue

Source Tissue Comment Organism Textmining
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme plays an essential role in fertilization of Halocynthia roretzi Halocynthia roretzi ?
-
 ?
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 ?
-
 ?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarin 7-amide + H2O
-
 Halocynthia roretzi tert-butyloxycarbonyl-Val-Pro + Arg-4-methylcoumarin-7-amide
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5 9
-
 Halocynthia roretzi

pI Value

Organism Comment pI Value Maximum pI Value
Halocynthia roretzi
-
-
 6.5