Information on EC 3.4.24.49 - bothropasin

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The expected taxonomic range for this enzyme is: Viperidae

EC NUMBER
COMMENTARY hide
3.4.24.49
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RECOMMENDED NAME
GeneOntology No.
bothropasin
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of His5-/-Leu, His10-/-Leu, Ala14-/-Leu, Tyr16-/-Leu and Phe24-/-Phe in insulin B chain
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
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CAS REGISTRY NUMBER
COMMENTARY hide
84788-89-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
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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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
casein + H2O
?
show the reaction diagram
casein + H2O
hydrolyzed casein
show the reaction diagram
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endopeptidase
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collagen I + H2O
?
show the reaction diagram
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-
-
-
?
Collagen IV + H2O
?
show the reaction diagram
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-
-
-
?
collagen VI + H2O
?
show the reaction diagram
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from human placenta
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-
?
Fibrin + H2O
?
show the reaction diagram
fibrinogen
?
show the reaction diagram
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-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
fibrinonectin + H2O
?
show the reaction diagram
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from human plasma
-
-
?
fibronectin
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
gelatin
?
show the reaction diagram
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-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
show the reaction diagram
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cleavage of His5-Leu, His10-Leu, Ala14-Leu, Tyr16-Leu and Phe24-Phe
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Matrigel + H2O
?
show the reaction diagram
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-
-
-
?
type I collagen
?
show the reaction diagram
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-
-
-
?
Vitronectin + H2O
?
show the reaction diagram
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from human plasma
-
-
?
von Willebrand factor + H2O
?
show the reaction diagram
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-
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Fibrin + H2O
?
show the reaction diagram
Q9PRP9
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
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-
?
Fibrinogen + H2O
?
show the reaction diagram
Q9PRP9
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-
-
?
Fibronectin + H2O
?
show the reaction diagram
additional information
?
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comparison of hemorrhagic, caseinolytic and fibrinogenolytic activities of metalloproteinases HF3, bothropasin, the DC protein and metalloproteinase BJ-PI. Hemorrhagic activity of bothropasin is 0.006 mg to produce a hemorrhagic area of 1 cm2. Fibrinogenolytic activity of bothropasin is 9.8 units/mg
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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1 mM required for maximal activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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by 2 mM
DTT
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by 2 mM
oxalate
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85% inhibition, restorage of 85% of activity by removal of oxalate by addition of Ca2+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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assay at
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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assay at
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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inside secretory vesicles and lumina
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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x * 37300, Bothrops jararaca, SDS-PAGE in presence of EDTA, x * 48000, Bothrops jararaca, SDS-PAGE
additional information
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bothropasin is aof P-III class and has a minor carbohydrate moiety and disintegrin-like/cysteine-rich domains
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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N-deglycosylation causes loss of structural stability of bothropasin
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+ stabilizes
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N-deglycosylation causes loss of structural stability of bothropasin
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
simplified procedure for the isolation of metalloproteinases HF3, bothropasin, the DC protein and metalloproteinase BJ-PI
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine