Isolation and cloning of a metalloproteinase from king cobra snake venom
Guo, X.; Zeng, L.; Lee, W.; Zhang, Y.; Jin, Y.; Toxicon 49, 954-965 (2007) 
Data extracted from this reference:
Cloned(Commentary)
Cloned (Commentary)
Organism
DNA and amino acid sequence determination and analysis, phylogenetic tree
Ophiophagus hannah
Inhibitors
Inhibitors
Commentary
Organism
Structure
EDTA
complete inhibition
Ophiophagus hannah
additional information
no inhibition by PMSF
Ophiophagus hannah
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
extracellular
-
Ophiophagus hannah
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
metalloproteinase
Ophiophagus hannah
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
47344
-
1 * 50000, SDS-PAGE, 1 * 47344, sequence calculation
Ophiophagus hannah
50000
-
1 * 50000, SDS-PAGE, 1 * 47344, sequence calculation
Ophiophagus hannah
55000
-
gel filtration
Ophiophagus hannah
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
Fibrinogen + H2O
Ophiophagus hannah
human substrate, specific degradation of the alpha-chain, no activity with beta-chain and gamma-chain, the enzyme has a fibrinogenolytic activity and hemorrhagic activity in mice, overview
?
-
-
?
additional information
Ophiophagus hannah
the enzyme inhibits platelet aggregation induced by ADP, TMVA, and stejnulxin
?
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Ophiophagus hannah
A3R0T9
king cobra
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
glycoprotein
ohagin contains four potential N-glycosylation sites
Ophiophagus hannah
Purification (Commentary)
Purification (Commentary)
Organism
native enzyme by gel filtration, ion exchange and heparin affinity chromatography
Ophiophagus hannah
Source Tissue
Source Tissue
Commentary
Organism
Textmining
venom
-
Ophiophagus hannah
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
hemorrhagic activity in mice, overview
Ophiophagus hannah
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
Fibrinogen + H2O
human substrate, specific degradation of the alpha-chain, no activity with beta-chain and gamma-chain, the enzyme has a fibrinogenolytic activity and hemorrhagic activity in mice, overview
684092
Ophiophagus hannah
?
-
-
-
?
Fibrinogen + H2O
specific degradation of the alpha-chain of the human substrate, while the beta- and gamma-chains are not hydrolyzed
684092
Ophiophagus hannah
?
-
-
-
?
additional information
the enzyme inhibits platelet aggregation induced by ADP, TMVA, and stejnulxin
684092
Ophiophagus hannah
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 50000, SDS-PAGE, 1 * 47344, sequence calculation
Ophiophagus hannah
More
MALDI-TOF enzyme peptide mass fingerprinting, the enzyme contains a signal peptide, a proprotein, and a metalloproteinase, a disintegrin-like, and a cysteine-rich domain, overview
Ophiophagus hannah
Synonyms
Synonyms
Commentary
Organism
ohagin
-
Ophiophagus hannah
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Ophiophagus hannah
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.6
-
assay at
Ophiophagus hannah
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Ophiophagus hannah
sequence calculation
-
5.84
Cloned(Commentary) (protein specific)
Commentary
Organism
DNA and amino acid sequence determination and analysis, phylogenetic tree
Ophiophagus hannah
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
EDTA
complete inhibition
Ophiophagus hannah
additional information
no inhibition by PMSF
Ophiophagus hannah
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
extracellular
-
Ophiophagus hannah
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
metalloproteinase
Ophiophagus hannah
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
47344
-
1 * 50000, SDS-PAGE, 1 * 47344, sequence calculation
Ophiophagus hannah
50000
-
1 * 50000, SDS-PAGE, 1 * 47344, sequence calculation
Ophiophagus hannah
55000
-
gel filtration
Ophiophagus hannah
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
Fibrinogen + H2O
Ophiophagus hannah
human substrate, specific degradation of the alpha-chain, no activity with beta-chain and gamma-chain, the enzyme has a fibrinogenolytic activity and hemorrhagic activity in mice, overview
?
-
-
?
additional information
Ophiophagus hannah
the enzyme inhibits platelet aggregation induced by ADP, TMVA, and stejnulxin
?
-
-
?
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
glycoprotein
ohagin contains four potential N-glycosylation sites
Ophiophagus hannah
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme by gel filtration, ion exchange and heparin affinity chromatography
Ophiophagus hannah
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
venom
-
Ophiophagus hannah
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
hemorrhagic activity in mice, overview
Ophiophagus hannah
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
Fibrinogen + H2O
human substrate, specific degradation of the alpha-chain, no activity with beta-chain and gamma-chain, the enzyme has a fibrinogenolytic activity and hemorrhagic activity in mice, overview
684092
Ophiophagus hannah
?
-
-
-
?
Fibrinogen + H2O
specific degradation of the alpha-chain of the human substrate, while the beta- and gamma-chains are not hydrolyzed
684092
Ophiophagus hannah
?
-
-
-
?
additional information
the enzyme inhibits platelet aggregation induced by ADP, TMVA, and stejnulxin
684092
Ophiophagus hannah
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 50000, SDS-PAGE, 1 * 47344, sequence calculation
Ophiophagus hannah
More
MALDI-TOF enzyme peptide mass fingerprinting, the enzyme contains a signal peptide, a proprotein, and a metalloproteinase, a disintegrin-like, and a cysteine-rich domain, overview
Ophiophagus hannah
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Ophiophagus hannah
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.6
-
assay at
Ophiophagus hannah
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Ophiophagus hannah
sequence calculation
-
5.84
Other publictions for EC 3.4.24.51
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)
684092
Guo
Isolation and cloning of a met ...
Ophiophagus hannah
Toxicon
49
954-965
2007
-
-
1
-
-
-
2
-
1
1
3
2
-
9
-
1
1
-
-
2
1
-
3
2
1
1
-
-
-
1
-
-
-
-
1
-
-
-
1
-
-
-
-
-
2
-
-
1
1
3
2
-
-
1
1
-
2
1
-
3
2
1
-
-
-
1
-
-
1
-
-
-
-
-
-
668853
Yamakawa
-
Ophiolysin ...
Ophiophagus hannah
Handbook Of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
699-701
2004
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-
-
-
-
-
2
-
-
-
2
-
-
1
-
-
1
-
-
1
-
-
2
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
1
-
1
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
31292
Yamakawa
A protease in the venom of kin ...
Ophiophagus hannah
Toxicon
26
1145-1155
1988
-
-
-
-
-
-
5
-
-
1
2
-
-
1
-
-
1
-
-
1
-
-
1
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
1
2
-
-
-
-
1
-
1
-
-
1
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-