BRENDA - Enzyme Database
show all sequences of 3.4.24.49

The three-dimensional structure of bothropasin, the main hemorrhagic factor from Bothrops jararaca venom: insights for a new classification of snake venom metalloprotease subgroups

Muniz, J.R.; Ambrosio, A.L.; Selistre-de-Araujo, H.S.; Cominetti, M.R.; Moura-da-Silva, A.M.; Oliva, G.; Garratt, R.C.; Souza, D.H.; Toxicon 52, 807-816 (2008)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
in complex with the inhibitor POL647. The catalytic domain consists of a scaffold of two subdomains organized similarly to those described for other snake venom metalloproteinases, including the zinc and calcium-binding sites. The free cysteine residue Cys189 is located within a hydrophobic core and it is not available for disulfide bonding or other interactions. There is no identifiable secondary structure for the disintegrin domain, instead it is composed mostly of loops stabilized by seven disulfide bonds and by two calcium ions. The ECD region is in a loop and is structurally related to the RGD region of RGD disintegrins. The ECD motif is stabilized by the Cys277-Cys310 disulfide bond between the disintegrin and cysteine-rich domains and by one calcium ion. The side chain of Glu276 of the ECD motif is exposed to solvent and free to make interactions. The hyper-variable region described for other PIII snake venom metalloproteinases in the cysteine-rich domain, presents a well-conserved sequence in bothropasin
Bothrops jararaca
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bothrops jararaca
O93523
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-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
Crystallization (Commentary) (protein specific)
Crystallization
Organism
in complex with the inhibitor POL647. The catalytic domain consists of a scaffold of two subdomains organized similarly to those described for other snake venom metalloproteinases, including the zinc and calcium-binding sites. The free cysteine residue Cys189 is located within a hydrophobic core and it is not available for disulfide bonding or other interactions. There is no identifiable secondary structure for the disintegrin domain, instead it is composed mostly of loops stabilized by seven disulfide bonds and by two calcium ions. The ECD region is in a loop and is structurally related to the RGD region of RGD disintegrins. The ECD motif is stabilized by the Cys277-Cys310 disulfide bond between the disintegrin and cysteine-rich domains and by one calcium ion. The side chain of Glu276 of the ECD motif is exposed to solvent and free to make interactions. The hyper-variable region described for other PIII snake venom metalloproteinases in the cysteine-rich domain, presents a well-conserved sequence in bothropasin
Bothrops jararaca
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
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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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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718413
Oliveira
New insights into the structur ...
Bothrops jararaca
Thromb. Haemost.
104
485-497
2010
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1
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2
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701331
Oliveira
Simplified procedures for the ...
Bothrops jararaca
Toxicon
53
797-801
2009
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701329
Muniz
The three-dimensional structur ...
Bothrops jararaca
Toxicon
52
807-816
2008
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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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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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31290
Mandelbaum
Isolation and characterization ...
Bothrops jararaca
Toxicon
20
955-972
1982
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