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 ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aggrecanase
-
-
Crotalus atrox metalloendopeptidase c
-
-
-
-
hemorrhagic metalloproteinase HT-d
-
-
Hemorrhagic toxin c and d
-
-
-
-
Hemorrhagic toxin c and d
-
-
PI metalloproteinase
-
-
Ruberlysin
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
158886-17-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
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 ACCESSION NO.
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
-
-
-
-
-
Fibronectin + H2O
?
show the reaction diagram
-
not
-
-
-
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 ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
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
-
-
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00015
-
tissue inhibitor of metalloproteinase 3
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20500
-
-
Crotalus atrox, isozyme Ht-c, gel filtration
21000
-
-
Crotalus atrox, isozyme Ht-d, gel filtration
23230
-
-
Crotalus atrox, isozyme Ht-d
24000
-
-
SDS-PAGE
27900
-
-
Crotalus atrox, minimal MW calculated from zinc content
additional information
-
-
they differ by a single amino acid substitution at position 181, Ala (Cc) or Asp (Cd)
additional information
-
-
amino acid composition
additional information
-
-
amino acid composition; isozymes Cc and Cd share identical antigenic structures
additional information
-
-
amino acid composition; they differ by a single amino acid substitution at position 181, Ala (Cc) or Asp (Cd)
additional information
-
-
amino acid composition; amino acid sequence (81% identity of toxins HT-2 and Ht-d)
additional information
-
-
amino acid composition
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
monomer
-
1 * 24000, Crotalus atrox; SDS-PAGE
monomer
-
Crotalus ruber ruber, toxin HT-2; SDS-PAGE
monomer
-
1 * 25000, Crotalus ruber ruber, toxin HT-2; 1 * 25500, Crotalus ruber ruber, toxin HT-3
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
no glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Crotalus atrox, crystallographic parameters
-
X-ray structure of atrolysin C, form D
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
70
-
-
inactivation
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
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