Information on EC 3.4.24.49 - bothropasin

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The expected taxonomic range for this enzyme is: Bothrops jararaca

EC NUMBER
COMMENTARY
3.4.24.49
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RECOMMENDED NAME
GeneOntology No.
bothropasin
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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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-
-
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REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Bothrops jararaca snake venom metalloproteinase
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Proteinase, Bothrops jararaca venom metallo-
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-
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CAS REGISTRY NUMBER
COMMENTARY
84788-89-6
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
adults of both sexes, 100-300 g
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-
Manually annotated by BRENDA team
jararaca snake
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
haemorrhagic effect of bothropasin on mouse skin, overview
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
casein + H2O
hydrolyzed casein
show the reaction diagram
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endopeptidase
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casein + H2O
?
show the reaction diagram
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enzyme stabilized by CaCl2
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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
-
-
?
Fibrin + H2O
?
show the reaction diagram
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-
-
-
?
fibrinogen
?
show the reaction diagram
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-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
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-
-
-
?
fibrinonectin + H2O
?
show the reaction diagram
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from human plasma
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-
?
fibronectin
?
show the reaction diagram
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-
-
-
?
gelatin
?
show the reaction diagram
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-
-
-
?
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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-
type I collagen
?
show the reaction diagram
-
-
-
-
?
Vitronectin + H2O
?
show the reaction diagram
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from human plasma
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-
?
von Willebrand factor + H2O
?
show the reaction diagram
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-
-
-
?
Matrigel + H2O
?
show the reaction diagram
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-
-
-
?
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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additional information
?
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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
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
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1 mM required for maximal activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
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by 2 mM
EDTA
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complete inhibition
EGTA
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complete inhibition
oxalate
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85% inhibition, restorage of 85% of activity by removal of oxalate by addition of Ca2+
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
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assay at
7.5
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assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
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assay at
37
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-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
inside secretory vesicles and lumina
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37300
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Bothrops jararaca, sedimentation equilibrium centrifugation in presence of EDTA
37300
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denatured and reduced protein in the presence of EDTA, SDS-PAGE, sedimentation equilibrium
48000
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SDS-PAGE
49870
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Bothrops jararaca, sedimentation equilibrium centrifugation in presence of 6 M guanidine-HCl and 0.1 M 2-mercaptoethanol
49870
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sedimentation equilibrium
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
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N-deglycosylation causes loss of structural stability of bothropasin
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
Ca2+ stabilizes
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N-deglycosylation causes loss of structural stability of bothropasin
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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
simplified procedure for the isolation of metalloproteinases HF3, bothropasin, the DC protein and metalloproteinase BJ-PI
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
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local tissue damage after snakebite, causes hemorrhage followed by myonecrosis and arterial necrosis after intramuscular injection of doses of 0.02 mg in mice, myonecrosis is still observed with lower doses down to 0.001 mg
medicine
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secretory cells of venom gland can be a good in vitro apparatus to produce venom, assemblage of isolated cells into acini that grow in size up to 21 days, instead of adhering to the substrate, source for all pharmacological and biotechnological studies, as well as providing an improved avenue for treatments of snakebites, venom detection and quantification after 2 weeks only in culture devoid of Bothrops jararaca serum