BRENDA - Enzyme Database
show all sequences of 3.4.21.99

Spermosin, a trypsin-like protease from ascidian sperm: cDNA cloning, protein structures and functional analysis

Kodama, E.; Baba, T.; Kohno, N.; Satoh, S.; Yokosawa, H.; Sawada, H.; Eur. J. Biochem. 269, 657-663 (2002)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
-
Halocynthia roretzi
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
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
?
-
Halocynthia roretzi
?
Organism
Organism
UniProt
Commentary
Textmining
Halocynthia roretzi
Q966V2
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
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 (Commentary)
Organism
-
Halocynthia roretzi
Source Tissue
Source Tissue
Commentary
Organism
Textmining
gonad
-
Halocynthia roretzi
-
additional information
no activity detected in hepatopancreas, intestine and brachial basket
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 binds to the vitelline coat plays a key role in sperm penetration through the vitelline coat during ascidian fertilization
651146
Halocynthia roretzi
?
-
651146
Halocynthia roretzi
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarin 7-amide + H2O
-
651146
Halocynthia roretzi
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
651146
Halocynthia roretzi
?
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Halocynthia roretzi
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
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
?
-
Halocynthia roretzi
?
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
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) (protein specific)
Commentary
Organism
-
Halocynthia roretzi
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
gonad
-
Halocynthia roretzi
-
additional information
no activity detected in hepatopancreas, intestine and brachial basket
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 binds to the vitelline coat plays a key role in sperm penetration through the vitelline coat during ascidian fertilization
651146
Halocynthia roretzi
?
-
651146
Halocynthia roretzi
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarin 7-amide + H2O
-
651146
Halocynthia roretzi
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
651146
Halocynthia roretzi
?
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
-
-
-
-
-
1
13
1
-
1
2
1
-
1
-
1
1
-
-
1
-
-
3
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
1
-
13
-
1
-
1
2
1
-
-
1
1
-
1
-
-
3
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
651146
Kodama
Spermosin, a trypsin-like prot ...
Halocynthia roretzi
Eur. J. Biochem.
269
657-663
2002
-
-
1
-
-
-
-
-
-
-
2
1
-
2
-
1
1
-
-
3
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
1
-
-
1
1
-
3
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
137256
Sawada
Localization, expression, and ...
Halocynthia roretzi
Biochem. Biophys. Res. Commun.
222
499-504
1996
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
137257
Sawada
Substrate specificity of ascid ...
Halocynthia roretzi
Mol. Reprod. Dev.
45
240-243
1996
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
137258
Sawada
-
Timing of action of sperm prot ...
Halocynthia roretzi
Experientia
42
74-75
1986
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
137254
Sawada
Purification and characterizat ...
Halocynthia roretzi
J. Biol. Chem.
259
2900-2904
1984
-
-
-
-
-
3
12
1
-
2
1
-
-
4
-
-
1
-
-
4
1
-
1
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
3
-
12
-
1
-
2
1
-
-
-
-
1
-
4
1
-
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
137255
Sawada
Evidence for the participation ...
Halocynthia roretzi
Dev. Biol.
105
246-249
1984
-
-
-
-
-
-
9
-
-
-
-
-
-
3
-
-
-
-
-
3
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
9
-
-
-
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-