Information on EC 3.4.24.46 - adamalysin

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The expected taxonomic range for this enzyme is: Amniota

EC NUMBER
COMMENTARY hide
3.4.24.46
-
RECOMMENDED NAME
GeneOntology No.
adamalysin
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of Phe1-/-Val, His5-/-Leu, His10-/-Leu, Ala14-/-Leu, Leu15-/-Tyr, and Tyr16-/-Leu of insulin B chain
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY hide
74812-51-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Eastern diamondback rattlesnake
-
-
Manually annotated by BRENDA team
recombinant disintegrin domain of enzyme
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
casein + H2O
?
show the reaction diagram
-
-
-
-
-
hide powder azure + H2O
?
show the reaction diagram
-
-
-
-
-
Human antithrombin III + H2O
Hydrolyzed and inactivated antithrombin III
show the reaction diagram
human plasma alpha1-proteinase inhibitor + H2O
hydrolyzed and inactivated human plasma alpha1-proteinase inhibitor
show the reaction diagram
Oxidized insulin B-chain + H2O
?
show the reaction diagram
-
cleavage at Phe1-Val2, His5-Leu6, His10-Leu11, Ala14-Leu15, Leu15-Tyr16 and Tyr16-Leu17
-
-
-
Polyarginine + H2O
Hydrolyzed polyarginine
show the reaction diagram
-
-
chain length 6-12 amino acids, not arginine monomers
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Polylysine + H2O
Hydrolyzed polylysine
show the reaction diagram
-
-
chain length 6-12 amino acids, not lysine monomers
-
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
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
2 mM Zn2+ protects at 2 mM 2-mercaptoethanol, 2 mM Zn2+ partially protects at 10-50 mM 2-mercaptoethanol, 2 mM Ca2+ partially protects at 2-10 mM 2-mercaptoethanol, no protection at 50 mM 2-mercaptoethanol
Acetyl-Trp-Cys-Gly-Pro-NH2
-
-
alpha1-Macroglobulin
-
mechanism
-
cysteine
Fur-Leu-Trp-OH
-
-
Lys-Pro-Arg-Cys-Gly-Val-NH2
-
-
Lys-Thr-Phe-Thr-Ser-Cys
-
-
N-(furan-2-yl)carbonyl-L-leucyl-D-phosphotryptophan
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N-(furan-2-yl)carbonyl-L-leucyl-L-phosphotryptophan
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-
N-(furan-2-yl)carbonyl-Leu-Trp(P)-(OH)2
-
-
Pro-Lys-Met-Cys-Gly-Val-NH2
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strong
Pro-Lys-Met-D-Cys-Gly-Val-NH2
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less effective than Pro-Lys-Met-Cys-Gly-Val-NH2
Pro-Lys-Met-Ser-Gly-Val-NH2
-
weak
PyroGlu-Asn-Trp
-
naturally found endogenous venom tripeptide inhibitor
additional information
-
no inhibition by diisopropyl fluorophosphate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heparin
-
activation, acceleration of antithrombin III inactivation, at a ratio of 6.7:1 (w/w)
additional information
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activation of inactive adamalysin II zymogen by cystein-switch-like mechanism
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
alkaline assay conditions
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
-
assay at
25
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22400
-
Crotalus adamanteus, sedimentation equilibrium centrifugation
23750
-
Crotalus adamanteus, calculated from amino acid content
24000
-
Crotalus adamanteus, PAGE
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 24000, Crotalus adamanteus, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complex with phosphate inhibitor, crystals obtained by sitting drop vapour diffusion technique, space group P3(2)12, cell parameters a : b : 73.5 A, c : 96.9 A
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Crotalus adamanteus
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Crotalus adamanteus; structure
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crystal structure in complex with 2 inhibitors
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, in 0.05 M sodium borate, pH 8, 2 mM CaCl2, at least 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
recombinant disintegrin domain of enzyme, shows inhibitory activities on endothelial cell proliferation and adhesion on the integrin substrates fibronectin, vitronectin, and fibrinogen.The domain totally abrogates endothelial cell migration and blocks most capillary formation in a three-dimensional fibrin gel. Athymic mice bearing electrotransferred domain exhibit strong inhibition of tumor angiogenesis
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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recombinant disintegrin domain of enzyme, shows inhibitory activities on endothelial cell proliferation and adhesion on the integrin substrates fibronectin, vitronectin, and fibrinogen.The domain totally abrogates endothelial cell migration and blocks most capillary formation in a three-dimensional fibrin gel. Athymic mice bearing electrotransferred domain exhibit strong inhibition of tumor angiogenesis