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Information on EC 3.4.24.49 - bothropasin and Organism(s) Bothrops jararaca and UniProt Accession O93523

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.49 bothropasin
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This record set is specific for:
Bothrops jararaca
UNIPROT: O93523 not found.
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Word Map
The taxonomic range for the selected organisms is: Bothrops jararaca
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Cleavage of His5-/-Leu, His10-/-Leu, Ala14-/-Leu, Tyr16-/-Leu and Phe24-/-Phe in insulin B chain
Synonyms
snake venom metalloproteinase, bothropasin, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Bothrops jararaca snake venom metalloproteinase
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Proteinase, Bothrops jararaca venom metallo-
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
84788-89-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Fibrinogen + H2O
?
show the reaction diagram
identification of peptides generated by bothropasin proteolytic activity. Among the fibrinogen derived peptides identified by mass spectrometry, analogous of endogenous products like the fibrinopeptides A and B are found, as well as other sequences described in the literature with vasoactive or antiangiogenic properties
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-
?
Fibronectin + H2O
?
show the reaction diagram
identification of peptides generated by bothropasin proteolytic activity. For most of the peptides no biological activity is described. Exceptionally a peptide that is known as a bond site for B cells is found
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-
?
casein + H2O
?
show the reaction diagram
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enzyme stabilized by CaCl2
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-
?
casein + H2O
hydrolyzed casein
show the reaction diagram
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endopeptidase
-
?
collagen I + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen IV + H2O
?
show the reaction diagram
-
-
-
-
?
collagen VI + H2O
?
show the reaction diagram
-
from human placenta
-
-
?
Fibrin + H2O
?
show the reaction diagram
-
-
-
-
?
fibrinogen
?
show the reaction diagram
-
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
-
-
-
?
fibrinonectin + H2O
?
show the reaction diagram
-
from human plasma
-
-
?
fibronectin
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
?
gelatin
?
show the reaction diagram
-
-
-
-
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
show the reaction diagram
-
cleavage of His5-Leu, His10-Leu, Ala14-Leu, Tyr16-Leu and Phe24-Phe
-
?
Matrigel + H2O
?
show the reaction diagram
-
-
-
-
?
type I collagen
?
show the reaction diagram
-
-
-
-
?
Vitronectin + H2O
?
show the reaction diagram
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from human plasma
-
-
?
von Willebrand factor + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Fibronectin + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
zinc-dependent enzyme
Ca2+
-
1 mM required for maximal activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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by 2 mM
DTT
-
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
-
assay at
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
inside secretory vesicles and lumina
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
beyond to the degradation of human proteins, bothropasin can generate bioactive peptides, which may participate in the envenoming process by Bothrops snakes
physiological function
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
VM3BP_BOTJA
610
0
68213
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37300
48000
49870
SUBUNIT
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
-
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
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mandelbaum, F.R.; Reichel, A.P.; Assakura, M.T.
Isolation and characterization of a proteolytic enzyme from the venom of the snake Bothrops jararaca (Jararaca)
Toxicon
20
955-972
1982
Bothrops jararaca
Manually annotated by BRENDA team
Mandelbaum, F.R.; Assakura, M.T.; Reichl, A.P.; Serrano, S.M.
Bothropasin
Handbook Of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
658-659
2004
Bothrops jararaca
-
Manually annotated by BRENDA team
Carneiro, S.M.; Zablith, M.B.; Kerchove, C.M.; Moura-da-Silva, A.M.; Quissell, D.O.; Markus, R.P.; Yamanouye, N.
Venom production in long-term primary culture of secretory cells of the Bothrops jararaca venom gland
Toxicon
47
87-94
2006
Bothrops jararaca
Manually annotated by BRENDA team
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.
The three-dimensional structure of bothropasin, the main hemorrhagic factor from Bothrops jararaca venom: insights for a new classification of snake venom metalloprotease subgroups
Toxicon
52
807-816
2008
Bothrops jararaca (O93523), Bothrops jararaca
Manually annotated by BRENDA team
Oliveira, A.K.; Paes Leme, A.F.; Assakura, M.T.; Menezes, M.C.; Zelanis, A.; Tashima, A.K.; Lopes-Ferreira, M.; Lima, C.; Camargo, A.C.; Fox, J.W.; Serrano, S.M.
Simplified procedures for the isolation of HF3, bothropasin, disintegrin-like/cysteine-rich protein and a novel P-I metalloproteinase from Bothrops jararaca venom
Toxicon
53
797-801
2009
Bothrops jararaca (O93523), Bothrops jararaca
Manually annotated by BRENDA team
Oliveira, A.K.; Paes Leme, A.F.; Asega, A.F.; Camargo, A.C.; Fox, J.W.; Serrano, S.M.
New insights into the structural elements involved in the skin haemorrhage induced by snake venom metalloproteinases
Thromb. Haemost.
104
485-497
2010
Bothrops jararaca
Manually annotated by BRENDA team
Paes Leme, A.; Sherman, N.; Smalley, D.; Sizukusa, L.; Oliveira, A.; Menezes, M.; Fox, J.; Serrano, S.
Hemorrhagic activity of HF3, a snake venom metalloproteinase: Insights from the proteomic analysis of mouse skin and blood plasma
J. Proteome Res.
11
279-291
2012
Bothrops jararaca (Q98UF9), Bothrops jararaca
Manually annotated by BRENDA team
Silva, C.C.F.; Menezes, M.C.; Palomino, M.; Oliveira, A.K.; Iwai, L.K.; Faria, M.; Portaro, F.V.
Peptides derived from plasma proteins released by bothropasin, ametalloprotease present in the Bothrops jararaca venom
Toxicon
137
65-72
2017
Bothrops jararaca (O93523), Bothrops jararaca
Manually annotated by BRENDA team