BRENDA - Enzyme Database
show all sequences of 3.4.24.49

Novel apigenin based small molecule that targets snake venom metalloproteases

Srinivasa, V.; Sundaram, M.; Anusha, S.; Hemshekhar, M.; Nayaka, S.; Kemparaju, K.; Basapp, B.; Girish, K.; Rangappa, K.; PLoS ONE 9, e106364 (2014)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
Fibrin + H2O
Echis carinatus
the enzyme specifically cleaves the alpha-polymer and alpha-chain of the fibrin molecule, in contrast gamma-gamma dimer and beta-chain of the fibrin are found to be resistant to the enzyme
?
-
-
?
Fibrinogen + H2O
Echis carinatus
-
?
-
-
?
Fibronectin + H2O
Echis carinatus
-
?
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Echis carinatus
Q9PRP9
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
venom
-
Echis carinatus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
casein + H2O
-
735120
Echis carinatus
?
-
-
-
?
Fibrin + H2O
the enzyme specifically cleaves the alpha-polymer and alpha-chain of the fibrin molecule, in contrast gamma-gamma dimer and beta-chain of the fibrin are found to be resistant to the enzyme
735120
Echis carinatus
?
-
-
-
?
Fibrinogen + H2O
-
735120
Echis carinatus
?
-
-
-
?
Fibronectin + H2O
-
735120
Echis carinatus
?
-
-
-
?
Gelatin + H2O
-
735120
Echis carinatus
?
-
-
-
?
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
Fibrin + H2O
Echis carinatus
the enzyme specifically cleaves the alpha-polymer and alpha-chain of the fibrin molecule, in contrast gamma-gamma dimer and beta-chain of the fibrin are found to be resistant to the enzyme
?
-
-
?
Fibrinogen + H2O
Echis carinatus
-
?
-
-
?
Fibronectin + H2O
Echis carinatus
-
?
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
venom
-
Echis carinatus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
casein + H2O
-
735120
Echis carinatus
?
-
-
-
?
Fibrin + H2O
the enzyme specifically cleaves the alpha-polymer and alpha-chain of the fibrin molecule, in contrast gamma-gamma dimer and beta-chain of the fibrin are found to be resistant to the enzyme
735120
Echis carinatus
?
-
-
-
?
Fibrinogen + H2O
-
735120
Echis carinatus
?
-
-
-
?
Fibronectin + H2O
-
735120
Echis carinatus
?
-
-
-
?
Gelatin + H2O
-
735120
Echis carinatus
?
-
-
-
?
Other publictions for EC 3.4.24.49
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
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)
735120
Srinivasa
Novel apigenin based small mol ...
Echis carinatus
PLoS ONE
9
e106364
2014
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3
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1
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5
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1
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5
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734561
Paes Leme
Hemorrhagic activity of HF3, a ...
Bothrops jararaca
J. Proteome Res.
11
279-291
2012
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1
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4
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7
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1
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7
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1
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1
1
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718413
Oliveira
New insights into the structur ...
Bothrops jararaca
Thromb. Haemost.
104
485-497
2010
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1
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3
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1
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9
1
1
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1
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1
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1
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9
1
1
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1
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2
2
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701331
Oliveira
Simplified procedures for the ...
Bothrops jararaca
Toxicon
53
797-801
2009
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1
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3
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1
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3
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1
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1
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3
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1
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701329
Muniz
The three-dimensional structur ...
Bothrops jararaca
Toxicon
52
807-816
2008
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1
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3
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2
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2
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670967
Carneiro
Venom production in long-term ...
Bothrops jararaca
Toxicon
47
87-94
2006
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1
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1
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3
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668844
Mandelbaum
-
Bothropasin ...
Bothrops jararaca
Handbook Of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
658-659
2004
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1
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4
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6
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4
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6
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1
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31290
Mandelbaum
Isolation and characterization ...
Bothrops jararaca
Toxicon
20
955-972
1982
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1
3
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1
3
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3
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1
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3
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2
1
1
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