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show all sequences of 3.4.24.49

New insights into the structural elements involved in the skin haemorrhage induced by snake venom metalloproteinases

Oliveira, A.K.; Paes Leme, A.F.; Asega, A.F.; Camargo, A.C.; Fox, J.W.; Serrano, S.M.; Thromb. Haemost. 104, 485-497 (2010)

Data extracted from this reference:

General Stability
General Stability
Organism
N-deglycosylation causes loss of structural stability of bothropasin
Bothrops jararaca
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bothrops jararaca
-
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
glycoprotein
N-deglycosylation causes loss of structural stability of bothropasin
Bothrops jararaca
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
collagen I + H2O
-
718413
Bothrops jararaca
?
-
-
-
?
Collagen IV + H2O
-
718413
Bothrops jararaca
?
-
-
-
?
collagen VI + H2O
from human placenta
718413
Bothrops jararaca
?
-
-
-
?
Fibrinogen + H2O
-
718413
Bothrops jararaca
?
-
-
-
?
fibrinonectin + H2O
from human plasma
718413
Bothrops jararaca
?
-
-
-
?
Matrigel + H2O
-
718413
Bothrops jararaca
?
-
-
-
?
additional information
bothropasin degradation profiles of fibrinogen, fibronectin, vitronectin, von Willebrand factor, collagens IV and VI, laminin and Matrigel in comparison to the other three snake venom metalloproteinases of Bothrops jararaca, binding to plasma and extracellular matrix proteins, overview. Collagen I is degraded only by bothropasin
718413
Bothrops jararaca
?
-
-
-
-
Vitronectin + H2O
from human plasma
718413
Bothrops jararaca
?
-
-
-
?
von Willebrand factor + H2O
-
718413
Bothrops jararaca
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
bothropasin is aof P-III class and has a minor carbohydrate moiety and disintegrin-like/cysteine-rich domains
Bothrops jararaca
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Bothrops jararaca
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Bothrops jararaca
General Stability (protein specific)
General Stability
Organism
N-deglycosylation causes loss of structural stability of bothropasin
Bothrops jararaca
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
glycoprotein
N-deglycosylation causes loss of structural stability of bothropasin
Bothrops jararaca
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
collagen I + H2O
-
718413
Bothrops jararaca
?
-
-
-
?
Collagen IV + H2O
-
718413
Bothrops jararaca
?
-
-
-
?
collagen VI + H2O
from human placenta
718413
Bothrops jararaca
?
-
-
-
?
Fibrinogen + H2O
-
718413
Bothrops jararaca
?
-
-
-
?
fibrinonectin + H2O
from human plasma
718413
Bothrops jararaca
?
-
-
-
?
Matrigel + H2O
-
718413
Bothrops jararaca
?
-
-
-
?
additional information
bothropasin degradation profiles of fibrinogen, fibronectin, vitronectin, von Willebrand factor, collagens IV and VI, laminin and Matrigel in comparison to the other three snake venom metalloproteinases of Bothrops jararaca, binding to plasma and extracellular matrix proteins, overview. Collagen I is degraded only by bothropasin
718413
Bothrops jararaca
?
-
-
-
-
Vitronectin + H2O
from human plasma
718413
Bothrops jararaca
?
-
-
-
?
von Willebrand factor + H2O
-
718413
Bothrops jararaca
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
bothropasin is aof P-III class and has a minor carbohydrate moiety and disintegrin-like/cysteine-rich domains
Bothrops jararaca
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Bothrops jararaca
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Bothrops jararaca
General Information
General Information
Commentary
Organism
additional information
role of the non-catalytic domains of snake venom metalloproteinases, interaction of four snake venom metalloproteinases of different domain compositions and glycosylation levels, from Bothrops jararaca venom, with plasma and extracellular matrix proteins, overview
Bothrops jararaca
physiological function
haemorrhagic effect of bothropasin on mouse skin, overview
Bothrops jararaca
General Information (protein specific)
General Information
Commentary
Organism
additional information
role of the non-catalytic domains of snake venom metalloproteinases, interaction of four snake venom metalloproteinases of different domain compositions and glycosylation levels, from Bothrops jararaca venom, with plasma and extracellular matrix proteins, overview
Bothrops jararaca
physiological function
haemorrhagic effect of bothropasin on mouse skin, overview
Bothrops jararaca
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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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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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
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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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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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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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1
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31290
Mandelbaum
Isolation and characterization ...
Bothrops jararaca
Toxicon
20
955-972
1982
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