BRENDA - Enzyme Database
show all sequences of 3.4.21.99

Spermosin

Lindsay, L.L.; Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press 2, 1567-1569 (2004)
No PubMed abstract available

Data extracted from this reference:

General Stability
General Stability
Organism
stabilized by nonionic detergents (Brij 35, Tween 80 or Triton X-100) at 0.005%
Halocynthia roretzi
Inhibitors
Inhibitors
Commentary
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
Commentary
Organism
Structure
0.145
-
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarin 7-amide
pH 8.0
Halocynthia roretzi
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
1-10 mM, activates
Halocynthia roretzi
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Halocynthia roretzi
the enzyme plays an essential role in fertilization of Halocynthia roretzi
?
-
-
-
Organism
Organism
UniProt
Commentary
Textmining
Halocynthia roretzi
-
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
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 (Commentary)
Organism
-
Halocynthia roretzi
Source Tissue
Source Tissue
Commentary
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
additional information
the enzyme plays an essential role in fertilization of Halocynthia roretzi
665085
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
665085
Halocynthia roretzi
?
-
-
-
-
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarin 7-amide + H2O
-
665085
Halocynthia roretzi
tert-butyloxycarbonyl-Val-Pro + Arg-4-methylcoumarin-7-amide
-
-
-
?
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
9
-
Halocynthia roretzi
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Halocynthia roretzi
-
-
6.5
General Stability (protein specific)
General Stability
Organism
stabilized by nonionic detergents (Brij 35, Tween 80 or Triton X-100) at 0.005%
Halocynthia roretzi
Inhibitors (protein specific)
Inhibitors
Commentary
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] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.145
-
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarin 7-amide
pH 8.0
Halocynthia roretzi
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
1-10 mM, activates
Halocynthia roretzi
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Halocynthia roretzi
the enzyme plays an essential role in fertilization of Halocynthia roretzi
?
-
-
-
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
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) (protein specific)
Commentary
Organism
-
Halocynthia roretzi
Source Tissue (protein specific)
Source Tissue
Commentary
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) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
additional information
the enzyme plays an essential role in fertilization of Halocynthia roretzi
665085
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
665085
Halocynthia roretzi
?
-
-
-
-
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarin 7-amide + H2O
-
665085
Halocynthia roretzi
tert-butyloxycarbonyl-Val-Pro + Arg-4-methylcoumarin-7-amide
-
-
-
?
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
9
-
Halocynthia roretzi
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Halocynthia roretzi
-
-
6.5
Other publictions for EC 3.4.21.99
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
665085
Lindsay
-
Spermosin ...
Halocynthia roretzi
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
2
1567-1569
2004
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1
13
1
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1
2
1
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1
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1
1
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1
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3
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1
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1
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1
-
13
-
1
-
1
2
1
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1
1
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1
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3
-
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1
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1
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-
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-
651146
Kodama
Spermosin, a trypsin-like prot ...
Halocynthia roretzi
Eur. J. Biochem.
269
657-663
2002
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1
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2
1
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2
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1
1
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3
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2
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1
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1
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1
1
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3
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2
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137256
Sawada
Localization, expression, and ...
Halocynthia roretzi
Biochem. Biophys. Res. Commun.
222
499-504
1996
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137257
Sawada
Substrate specificity of ascid ...
Halocynthia roretzi
Mol. Reprod. Dev.
45
240-243
1996
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2
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2
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1
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137258
Sawada
-
Timing of action of sperm prot ...
Halocynthia roretzi
Experientia
42
74-75
1986
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1
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1
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1
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1
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1
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137254
Sawada
Purification and characterizat ...
Halocynthia roretzi
J. Biol. Chem.
259
2900-2904
1984
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3
12
1
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2
1
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4
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1
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4
1
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1
1
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1
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3
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12
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1
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2
1
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1
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4
1
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1
1
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1
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137255
Sawada
Evidence for the participation ...
Halocynthia roretzi
Dev. Biol.
105
246-249
1984
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9
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3
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3
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1
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9
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3
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1
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