Information on EC 3.4.24.44 - atrolysin E

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The expected taxonomic range for this enzyme is: Crotalus atrox

EC NUMBER
COMMENTARY hide
3.4.24.44
-
RECOMMENDED NAME
GeneOntology No.
atrolysin E
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of Asn3-/-Gln, Ser9-/-His and Ala14-/-Leu bonds in insulin B chain and Tyr14-/-Gln and Thr8-/-Ser in A chain. Cleaves type IV collagen at Ala73-/-Gln in alpha1(IV) and at Gly7-/-Leu in alpha2(IV)
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
172306-51-3
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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
Basement membrane preparation + H2O
Soluble peptides
show the reaction diagram
basement membrane preperation from Engel-breth-Holm-Swarm tumor + H2O
?
show the reaction diagram
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great proteolytic activity
-
-
?
Basement membranes surrounding capillaries + H2O
?
show the reaction diagram
collagen type IV + H2O
?
show the reaction diagram
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-
-
-
?
Collagen type IV alphaI(IV) chains + H2O
?
show the reaction diagram
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basement membrane component, cleavage at Ala219-Gln220
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-
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Collagen type IV alphaII(IV) chain + H2O
?
show the reaction diagram
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basement membrane component, cleavage at Thr228-Leu229
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-
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Dimethylcasein + H2O
?
show the reaction diagram
Dimethylhemoglobin + H2O
?
show the reaction diagram
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-
-
-
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Fibrinogen + H2O
?
show the reaction diagram
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rapid cleavage of the Aalpha chain followed by the Bbeta and gamma chains
-
-
?
Fibrinogen + H2O
Hydrolyzed fibrinogen
show the reaction diagram
Fibronectin + H2O
Hydrolyzed fibronectin
show the reaction diagram
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-
lower MW fragments
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Gelatin of collagen type I + H2O
?
show the reaction diagram
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-
-
-
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Gelatin of collagen type II + H2O
?
show the reaction diagram
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-
-
-
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Gelatin of collagen type III + H2O
?
show the reaction diagram
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-
-
-
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Gelatin of collagen type V + H2O
?
show the reaction diagram
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-
-
-
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Human alpha2-macroglobulin + H2O
?
show the reaction diagram
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cleavage at Val689-Met690 and Gly693-His694
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-
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Laminin + H2O
?
show the reaction diagram
Laminin/nidogen complex + H2O
?
show the reaction diagram
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cleavage at positions 322, 336, 351, 840 and 953
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Nidogen + H2O
?
show the reaction diagram
o-aminobenzoyl-Ala-Gly-Leu-Ala-nitrobenzylamide + H2O
?
show the reaction diagram
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-
-
-
?
Oxidized insulin A-chain + H2O
Hydrolyzed oxidized insulin A-chain
show the reaction diagram
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rapid cleavage at Tyr14-Gln15, more slowly at Ala8-Ser9, kinetics
peptides (Gln15-Asn21) + (Gly1-Tyr14) + (Ser9-Tyr14) + (Gly1-Ala8)
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Oxidized insulin B-chain + H2O
?
show the reaction diagram
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-
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
show the reaction diagram
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
Basement membranes surrounding capillaries + H2O
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
low concentrations stabilize proteolytic activity
additional information
-
metal analysis detects 0.42 mol Ca2+ and 0.05 mol Mg2+ per mol enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
alpha2-Macroglobulin
-
inhibits proteolytic and hemorrhagic activities
-
antihemorrhagins from serum of Crotalus atrox
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inhibits proteolytic and hemorrhagic activities
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Human plasma alpha2-macroglobulin
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Pyroglutamate peptides
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e.g. pyro-Glu-Asn-Trp or pyro-Glu-Glu-Trp
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synthetic carboxyalkyl peptide
-
effective inhibitor
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Synthetic peptide inhibitors with N-[1-(R,S)-carboxypentyl] moiety
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-
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venom-derived pyroglutamyl-containing peptide
-
effective inhibitor
-
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.167 - 0.217
dimethylcasein
-
0.00767 - 0.06
oxidized insulin A-chain
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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
3788
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MALDI-TOF
7312
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calculated from amino acid sequence
7392
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MALDI-TOF MS
7400
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atrolysin E disintegrin domain
16000
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atrolysin E/D, SDS-PAGE
22000
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Crotalus atrox, gel filtration
25000
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Crotalus atrox, minimum MW calculated from zinc content
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no glycoprotein
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
atrolysin E disintegrin
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from lyophilized crude venom
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ion-exchange chromatography and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA sequence analysis
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produced with a CMV expression vector in 293 cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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one of the most hemorrhagic metalloproteinases of the P-II class in the venom, causes extensive hemorrhage in muscle tissue and extensive degeneration of capillaries, degradation of basement membrane proteins and surrounding stroma, its free disintegrin domain possesses platelet-aggregation inhibitory activity