Information on EC 3.4.24.43 - atroxase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Crotalus atrox

EC NUMBER
COMMENTARY hide
3.4.24.43
-
RECOMMENDED NAME
GeneOntology No.
atroxase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of His5-/-Leu, Ser9-/-His, His10-/-Leu, Ala14-/-Leu and Tyr16-/-Leu of insulin B chain
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
165447-15-4
-
181186-94-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Dimethylcasein + H2O
?
show the reaction diagram
-
-
-
-
-
Fibrin + H2O
?
show the reaction diagram
-
both alpha and beta chains hydrolyzed, but the gamma-gamma chain not affected
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
Aalpha and Bbeta chains readily hydrolyzed, but gamma chain resistant to hydrolysis
-
-
?
Human fibrinogen + H2O
?
show the reaction diagram
Oxidized insulin B-chain
?
show the reaction diagram
-
cleavage of His5-Leu6, Ser9-His10, His10-Leu11, Ala14-Leu15, Tyr16-Leu17
-
-
-
Oxidized insulin B-chain + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
additional information
?
-
-
nontoxic venom component, nonhemorrhagic endopeptidase
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
0.3 mol/mol enzyme
K+
-
1 mol/mol enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha2-Macroglobulin
-
-
-
EDTA
-
Zn2+ protects
additional information
-
no inhibition by aprotinin, PMSF or soybean trypsin inhibitor
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
1.67 mg fibrinogen/min mg enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
pI: 9.6
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 23500, Crotalus atrox, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11
-
inactivation
31271
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
inactivation
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by cellulose column chromatography
-
from lyophilized crude venom
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Crotalus atrox, expressed in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
no necrosis or hemorrhage, thrombolysis