Information on EC 3.4.24.42 - atrolysin C

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The expected taxonomic range for this enzyme is: Crotalus

EC NUMBER
COMMENTARY
3.4.24.42
-
RECOMMENDED NAME
GeneOntology No.
atrolysin C
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cleavage of His5-/-Leu, His10-/-Leu, Ala14-/-Leu, Tyr16-/-Leu and Gly23-/-Phe bonds in B chain of insulin. With small molecule substrates prefers hydrophobic residue at P2' and small residue such as Ala, Gly at P1
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Crotalus atrox metalloendopeptidase c
-
-
-
-
Hemorrhagic toxin c and d
-
-
-
-
Ruberlysin
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
158886-17-0
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
rattlesnake
-
-
Manually annotated by BRENDA team
Western diamondback rattlesnake
-
-
Manually annotated by BRENDA team
red rattlesnake
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzyl amide + H2O
?
show the reaction diagram
-
-
-
-
-
2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzyl amide + H2O
?
show the reaction diagram
-
-
-
-
?
Acetyl-Val-Ala-Ala-Leu-Gly-Ala + H2O
?
show the reaction diagram
-
-
-
-
-
Acetyl-Val-Ala-Leu-Leu-Ala + H2O
?
show the reaction diagram
-
best substrate of synthetic acetylated pentapeptides
-
-
-
Angiotensin I + H2O
Asp-Arg-Val-Tyr-Ile-His + Pro + Phe-His-Leu
show the reaction diagram
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu, cleaved at His-Pro and Pro-Phe
-
-
azocoll
?
show the reaction diagram
-
-
-
-
?
Basement membrane preparation + H2O
Soluble peptides
show the reaction diagram
-
-
-
-
-
Basement membrane preparation + H2O
Soluble peptides
show the reaction diagram
-
poor substrate: component band a
-
-
Basement membranes surrounding capillaries + H2O
?
show the reaction diagram
-
involved in disruption of capillary membranes causing hemorrhage in surrounding tissue
-
-
-
Basement membranes surrounding capillaries + H2O
?
show the reaction diagram
-
together with hemorrhagic toxins a, b, e and f responsible for hemorrhage
-
-
-
Basement membranes surrounding capillaries + H2O
?
show the reaction diagram
-
together with atrolysins B and E member of the class P-I hemorrhagic toxins
-
-
-
Basement membranes surrounding capillaries + H2O
?
show the reaction diagram
-
less potent hemorrhagic toxins of Crotalus atrox venom
-
-
-
bovine aggrecan monomer + H2O
?
show the reaction diagram
-
-
-
?
bovine aggrecan monomer + H2O
?
show the reaction diagram
-
purified atrolysin C can cleave at the cleavage sites VIPEN + FFBVG and ITEGE + ARGSV independently
-
-
?
cartilage aggrecan + H2O
?
show the reaction diagram
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
-
Collagen type IV + H2O
Hydrolyzed collagen type IV
show the reaction diagram
-
basement membrane component, alpha1 (MW 185000) and alpha2 (MW 170000) chain
-
-
-
Collagen type IV + H2O
Hydrolyzed collagen type IV
show the reaction diagram
-
basement membrane component, alpha1 (MW 185000) and alpha2 (MW 170000) chain
MW 170000, MW 164000, MW 125000, MW 110000, MW 940000 and MW 64000 fragments
-
Dimethylcasein + H2O
?
show the reaction diagram
-
-
-
-
?
Dimethylcasein + H2O
?
show the reaction diagram
-
-
-
-
-
Fibrinogen + H2O
Hydrolyzed fibrinogen
show the reaction diagram
-
-
-
-
-
Fibrinogen + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
-
FSFRLT + H2O
?
show the reaction diagram
-
good substrate
-
-
?
Gelatin of collagen type I + H2O
Hydrolyzed gelatin of collagen type I
show the reaction diagram
-
i.e. denatured collagen
-
-
-
Gelatin of collagen type I + H2O
Hydrolyzed gelatin of collagen type I
show the reaction diagram
-
i.e. denatured collagen
MW 60000 and MW 50000 fragments
-
Gelatin of collagen type III + H2O
?
show the reaction diagram
-
i.e. denatured collagen
-
-
-
Gelatin of collagen type V + H2O
Hydrolyzed gelatin of collagen type V
show the reaction diagram
-
i.e. denatured collagen, hydrolysis at 38ųC and above, not below
MW 130000, MW 118000, MW 93000 and MW 85000 fragments
-
Glu-Ala-Leu-Tyr-Leu + H2O
?
show the reaction diagram
-
peptide derived from insulin B-chain
-
-
-
hide powder azure + H2O
?
show the reaction diagram
-
-
-
-
-
hide powder azure + H2O
?
show the reaction diagram
-
-
-
-
-
HTLRKA + H2O
?
show the reaction diagram
-
good substrate
-
-
?
Human alpha2-macroglobulin + H2O
?
show the reaction diagram
-
cleavage at Arg696-Leu697
-
-
-
IAQLNR + H2O
?
show the reaction diagram
-
good substrate
-
-
?
IPLRTV + H2O
?
show the reaction diagram
-
good substrate
-
-
?
Laminin + H2O
?
show the reaction diagram
-
-
-
-
-
Laminin + H2O
?
show the reaction diagram
-
basement membrane component, poor substrate
-
-
-
Leu-Val-Glu-Ala-Leu-Tyr-Leu + H2O
Leu-Val-Glu-Ala + Leu-Tyr-Leu
show the reaction diagram
-
cleavage at Ala-Leu
-
-
-
Leu-Val-Glu-Ala-Leu-Tyr-Leu + H2O
Leu-Val-Glu-Ala + Leu-Tyr-Leu
show the reaction diagram
-
peptide derived from insulin B-chain, best substrate
-
-
-
Luteinizing hormone-releasing hormone + H2O
?
show the reaction diagram
-
cleavage sites: Trp3-Ser4, Gly6-Leu7
-
-
-
Nidogen + H2O
?
show the reaction diagram
-
basement membrane component
-
-
-
Oxidized insulin B-chain + H2O
?
show the reaction diagram
-
-
-
-
-
Oxidized insulin B-chain + H2O
?
show the reaction diagram
-
-
-
-
?
Oxidized insulin B-chain + H2O
?
show the reaction diagram
-
cleavage at Gly23-Phe24
-
-
-
Oxidized insulin B-chain + H2O
?
show the reaction diagram
-
cleavage at Gly23-Phe24
-
-
-
Oxidized insulin B-chain + H2O
?
show the reaction diagram
-
cleavage at His5-Leu6, His10-Leu11, Ala14-Leu15 (most rapidly cleaved bond)
-
-
-
Oxidized insulin B-chain + H2O
?
show the reaction diagram
-
cleaves the same bonds as atrolysin B and A (the latter except Gly23-Phe24)
-
-
-
Oxidized insulin B-chain + H2O
?
show the reaction diagram
-
cleavage at Tyr16-Leu17 (slightly less rapidly cleaved bond)
-
-
-
Oxidized insulin B-chain + H2O
?
show the reaction diagram
-
Crotalus ruber ruber toxin HT-3 does not cleave the His5-Leu6 bond which is cleaved by HT-2
-
-
-
SFMRLS + H2O
?
show the reaction diagram
-
good substrate
-
-
?
TQRKRS + H2O
?
show the reaction diagram
-
good substrate
-
-
?
Val-Glu-Ala-Leu-Tyr-Leu + H2O
?
show the reaction diagram
-
peptide derived from insulin B-chain
-
-
-
von Willebrand factor + H2O
?
show the reaction diagram
-
VWF is a large, multidomain glycoprotein present in human blood and in the secretory granules of endothelial cells and platelets, i.e. VWF, is a large, multidomain glycoprotein, atrolysin C does not require specific interaction with the VWA1 domain and likely cleaves VWF in a nonlocalized manner, cleavage in sequences MSMG-/-VSG, MSMG(C)V-/-G, LVPDS-/-H, and MSMG(C)VSG, after the D domain and the cystine knot-like domain, atrolysin C cleaves VWF at widely distributed sites identified next to VWD3 and VWD4 domains, overview
-
-
?
Met-enkephalin + H2O
Tyr-Gly-Gly + Phe-Met
show the reaction diagram
-
i.e. Tyr-Gly-Gly-Phe-Met, cleavage site: Gly3-Phe4
-
-
-
additional information
?
-
-
no hydrolysis of fibrin
-
-
-
additional information
?
-
-
no hydrolysis of interstitial collagen, native type I collagen
-
-
-
additional information
?
-
-
no hydrolysis of peptide Ala-Leu-Tyr-Leu, cleavage specificity, compared to hemorrhagic toxins a and b
-
-
-
additional information
?
-
-
hemorrhagic and myonecrotic activity
-
-
-
additional information
?
-
-
substrate requirements: small aliphatic residues at P1 (Ala or Gly) and Leu at P2
-
-
-
additional information
?
-
-
substrate digestion patterns differ from those of atrolysins A and E
-
-
-
additional information
?
-
-
peptides of four residues or less are not hydrolyzed, no significant degradation of fibrin
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Basement membranes surrounding capillaries + H2O
?
show the reaction diagram
-
involved in disruption of capillary membranes causing hemorrhage in surrounding tissue
-
-
-
Basement membranes surrounding capillaries + H2O
?
show the reaction diagram
-
together with hemorrhagic toxins a, b, e and f responsible for hemorrhage
-
-
-
Basement membranes surrounding capillaries + H2O
?
show the reaction diagram
-
together with atrolysins B and E member of the class P-I hemorrhagic toxins
-
-
-
Basement membranes surrounding capillaries + H2O
?
show the reaction diagram
-
less potent hemorrhagic toxins of Crotalus atrox venom
-
-
-
von Willebrand factor + H2O
?
show the reaction diagram
-
VWF is a large, multidomain glycoprotein present in human blood and in the secretory granules of endothelial cells and platelets
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Na+
-
8.5 mol/mol toxin HT-3, 10.3 mol/mol toxin HT-2
Zn2+
-
1 mol zinc/mol enzyme; zinc metalloproteinase
Zn2+
-
0.86 mol zinc/mol enzyme; zinc metalloproteinase
Zn2+
-
zinc metalloproteinase
Zn2+
-
1 mol zinc/mol enzyme; zinc metalloproteinase
Zn2+
-
catalytic
Zn2+
-
zinc metalloprotease
Ca2+
-
0.75 mol/mol toxin HT-3, 1.1 mol/mol toxin HT-2
additional information
-
less than 0.3 mol Mg2+/mol toxin, less than 0.8 mol K+/mol toxin HT-3 and less than 0.9 mol K+/mol toxin HT-2
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
inhibits proteolytic and hemorrhagic activity of atrolysin C
Ala-Leu-Tyr-Leu
-
isozyme Ht-c
alpha2-Macroglobulin
-
-
-
alpha2-Macroglobulin
-
inhibits proteolytic and hemorrhagic activity of atrolysin C
-
Amino acid hydroxamates
-
-
Amino acid hydroxamates
-
isozyme Ht-c
amino acid hydroxymate
-
-
Benzyloxycarbonyl-Leu-Gly-NHOH
-
-
catrocollastatin C
-
-
-
chloromethyl ester
-
-
Collagenase inhibitor SC 44463
-
-
cysteine
-
-
EDTA
-
activity completely blocked
EDTA
-
inhibits proteolytic and hemorrhagic activity of atrolysin C
phosphoramidon
-
i.e. N-[L-rhamnopyranosyl-oxyhydroxyphosphinyl]-L-leucyl-L-tryptophan, isozyme Ht-c
phosphoramidon
-
weak, isozyme Ht-d
phosphoramidon
-
thermolysin inhibitor
Pyro-Glu-Asn-Trp
-
-
thiorphan
-
-
tissue inhibitor of metalloproteinase 3
-
N-terminal domain of the tissue inhibitor of metalloproteinase 3 is a potent inhibitor
-
Inhibitor SCH 47890
-
mechanism
additional information
-
acetyl-Ala-Val-Leu-Gly-Ala, acetyl-Val-Glu-Leu-Gly-Ala, acetyl-Val-Lys-Leu-Gly-Ala, acetyl-Lys-Ala-Leu-Gly-Ala, acetyl-Val-Ala-Ile-Gly-Ala, furylacryloyl-Gly-L-Leu-NH2
-
additional information
-
no inhibition by aprotinin, PMSF
-
additional information
-
iodoacetate; no inhibition by aprotinin, PMSF
-
additional information
-
benzamidine, tosyl-L-Phe chloromethyl ketone, soybean or egg white trypsin inhibitor or PCMB
-
additional information
-
tissue inhibitor of metalloproteinase 1 and tissue inhibitor of metalloproteinase 2 have no inhibitory activity
-
additional information
-
inhibitory protein in the serum of Bothrops jararaca
-
additional information
-
the isolated recombinant cysteine-rich domain of atrolysin A does not inhibit full-length atrolysin activity, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.71
acetyl-Ala-Ala-Leu-Gly-Ala
-
-
0.76
acetyl-Glu-Ala-Leu-Gly-Ala
-
isozyme Ht-c
0.69
Acetyl-Val-Ala-Ala-Leu-Gly-Ala
-
isozyme Ht-d
0.31
acetyl-Val-Ala-Leu-Gly-Gly
-
isozyme c, acetyl-Val-Ala-Leu-Gly-Ala, 2-aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzyl amide
0.45
acetyl-Val-Ala-Leu-Gly-Gly
-
isozyme Ht-c
0.62
Acetyl-Val-Ala-Leu-Leu-Ala
-
acetyl-Val-Ala-Ala-Leu-Gly-Ala, isozyme Ht-c
0.63
Acetyl-Val-Ala-Leu-Leu-Ala
-
isozyme Ht-d
0.5
acetyl-Val-Ala-Phe-Gly-Ala
-
isozyme Ht-c
0.21
acetyl-Val-Gly-Leu-Gly-Ala
-
isozyme Ht-c
0.14
Glu-Ala-Leu-Tyr-Leu
-
isozyme Ht-d
0.29
Glu-Ala-Leu-Tyr-Leu
-
isozyme Ht-c
0.032
Leu-Val-Glu-Ala-Leu-Tyr-Leu
-
isozyme Ht-d
0.11
Leu-Val-Glu-Ala-Leu-Tyr-Leu
-
isozyme Ht-c
0.023
Val-Glu-Ala-Leu-Tyr-Leu
-
isozyme Ht-d
0.12
Val-Glu-Ala-Leu-Tyr-Leu
-
isozyme Ht-c
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00015
tissue inhibitor of metalloproteinase 3
-
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
-
assay at
8.3
-
hide powder azure, isozyme Ht-c
9
-
hide powder azure, isozyme Ht-d
additional information
-
pI: 6 (isozyme Cc), pI: 6.1 (isozyme Cd)
additional information
-
pI: 6.1 (isozyme Ht-d); pI: 6.2 (isozyme Ht-c)
additional information
-
pI: 5.2 (toxin HT-2), pI: 9.6 (toxin HT-3)
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3 - 10
-
about half-maximal activity at pH 7.3 and 10, isozyme Ht-d
7.5 - 9.8
-
about half-maximal activity at pH 7.5 and 9.8, isozyme Ht-c
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
assay at
37
-
assay at
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20500
-
Crotalus atrox, isozyme Ht-c, gel filtration
31261
21000
-
Crotalus atrox, isozyme Ht-d, gel filtration
31261
23230
-
Crotalus atrox, isozyme Ht-d
31268
24000
-
SDS-PAGE
668846
27900
-
Crotalus atrox, minimal MW calculated from zinc content
31261
additional information
-
they differ by a single amino acid substitution at position 181, Ala (Cc) or Asp (Cd)
31259
additional information
-
amino acid composition
31261
additional information
-
amino acid composition; isozymes Cc and Cd share identical antigenic structures
31266
additional information
-
amino acid composition; they differ by a single amino acid substitution at position 181, Ala (Cc) or Asp (Cd)
31268
additional information
-
amino acid composition; amino acid sequence (81% identity of toxins HT-2 and Ht-d)
31270
additional information
-
amino acid composition
36970
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
SDS-PAGE
monomer
-
SDS-PAGE
monomer
-
1 * 24000, Crotalus atrox
monomer
-
Crotalus ruber ruber, toxin HT-2
monomer
-
1 * 25000, Crotalus ruber ruber, toxin HT-2, 1 * 25500, Crotalus ruber ruber, toxin HT-3
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Crotalus atrox, crystallographic parameters
-
X-ray structure of atrolysin C, form D
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
-
inactivation
36970
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
formerly Ht-c and Ht-d; from lyophilized crude venom; two isozymes Cc and Cd
-
from lyophilized crude venom
-
gel filtration, ion exchange chromatography
-
from lyophilized crude venom, toxins HT-2 and HT-3
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
P15167
molecular characteristics that influence the toxic effects of snake venom metalloproteases, subdivision in hemorrhagic and non-hemorrhagic snake venom metalloproteases