Information on EC 3.4.24.1 - atrolysin A

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The expected taxonomic range for this enzyme is: Crotalus

EC NUMBER
COMMENTARY hide
3.4.24.1
-
RECOMMENDED NAME
GeneOntology No.
atrolysin A
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of Asn3-/-Gln, His5-/-Leu, His10-/-Leu, Ala14-/-Leu and Tyr16-/-Leu in insulin B chain; removes C-terminal Leu from small peptides
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase; peptides, endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY hide
37288-82-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
red rattlesnake
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
recombinant protease inhibits platelet adhesion to fibrinogen with an estimated IC50 of 1 nM. It inhibits collagen- (IC50 is 18 nM) and ADP-induced (IC50 is 6 nM) platelet aggregation, and also inhibits platelet function on clot retraction
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha fibrinogen + H2O
?
show the reaction diagram
alpha1-Antichymotrypsin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha2-macroglobulin + H2O
?
show the reaction diagram
-
-
-
-
?
Angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
beta fibrinogen + H2O
?
show the reaction diagram
casein + H2O
?
show the reaction diagram
-
preferential cleavage: -Leu, -Ile, -Val, -Phe
-
-
?
demethylcasein + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
insulin B chain + H2O
?
show the reaction diagram
Laminin + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-Val-Glu-Ala-Leu-Tyr-Leu + H2O
?
show the reaction diagram
-
-
-
-
?
Nidogen + H2O
?
show the reaction diagram
-
-
-
-
?
Proteins + H2O
?
show the reaction diagram
Type I collagen + H2O
?
show the reaction diagram
-
enzyme binds via exosites in the cysteine-rich domain
-
-
?
Type IV collagen + H2O
?
show the reaction diagram
-
-
-
-
?
von Willebrand factor + H2O
?
show the reaction diagram
-
enzyme binds via exosites in the cysteine-rich domain
-
-
?
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
Proteins + H2O
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
-
requirement
Na+
-
requirement
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha1-Macroglobulin
-
-
-
Chloromethyl esters
-
-
CI-inhibitor
-
-
-
L-Ile-NHOH
-
-
L-Leu-CH2Cl
-
-
L-Leu-NHOH
-
-
L-Phe-NHOH
-
-
L-Val-NHOH
-
-
MeO-Suc-Gly-Leu-Phe-CH2Cl
-
-
Nalpha-p-tosyl-L-lysine chloromethyl ketone
-
-
Nalpha-p-tosyl-L-phenylalanine chloromethyl ketone
-
-
NH2-Ala-Leu-Tyr-Leu-COOH
-
-
o-phenanthroline
phenylmethanesulfonyl fluoride
-
-
phosphoramidon
-
-
additional information
-
not: phenylmethanesulfonyl fluoride, Nalpha-p-tosyl-L-phenylalanine chloromethyl ketone, Nalpha-p-tosyl-L-lysine chloromethyl ketone
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Crotalus atrox
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 9
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
-
pH 7 or pH 10: about 15% of activity maximum
7.5 - 11
-
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 70
-
0C, 70C: about 15% of activity maximum
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
cDNA generated from
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8000
x * 8000, calculated
21890
-
amino acid analysis
22000
-
1 * 22000, SDS-PAGE
23230
-
Ht-d, amino acid analysis
24800
-
1 * 24800, SDS-PAGE, HT-2
25000
-
HT-2, amino acid analysis
25500
-
HT-3, amino acid analysis
25700
-
1 * 25700, SDS-PAGE, HT-3
26000
-
? * 26000, SDS-PAGE
26740
-
amino acid analysis
30000
-
non-denaturing PAGE
60000
-
1 * 60000, SDS-PAGE, HT-1
60050
-
Ht-1, amino acid analysis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no modification
-
non-glycosylated
proteolytic modification
deduced amino acid sequence contains a signal peptide
side-chain modification
-
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
molecular modeling using the crystal structures of atrolysin C and adamalysin II as template structures; molecular modeling using the crystal structures of atrolysin C and adamalysin II as template structures; molecular modeling using the crystal structures of atrolysin C and adamalysin II as template structures
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
stable for 30 min
80
-
complete loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
18C, 18 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity purified
-
HT-1, HT-2 and HT-3
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned into the pGEM-T veactor and transformed in Escherichia coli
expression of recombinant cysteine-rich domain of atrolysin A in Escherichia coli
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expression of recombinant enzyme in Sf9/baculovirus
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
recombinant protease inhibits platelet adhesion to fibrinogen with an estimated IC50 of 1 nM. It inhibits collagen- (IC50 is 18 nM) and ADP-induced (IC50 is 6 nM) platelet aggregation, and also inhibits platelet function on clot retraction