HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 3.4.24.42 - atrolysin C
for references in articles please use BRENDA:EC3.4.24.42
Word Map on EC 3.4.24.42
- 3.4.24.42
- cartilage
-
articular
- osteoarthritis
- chondrocytes
- joint
-
metalloproteinases
-
proteoglycans
-
explants
- collagen
-
thrombospondin
- glycosaminoglycans
- adamts-4
- synovial
- knee
-
interglobular
-
disintegrin
-
neoepitope
-
arthritic
- chondroitin
-
aggrecanolysis
-
chondroprotective
-
nitege
-
timp-3
-
aggrecan-degrading
-
interleukin-1alpha
-
versican
-
matrix-degrading
- mannosamine
- adamalysin
- arthritides
-
mmp-mediated
-
meniscal
-
svmps
-
disintegrin-like
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Crotalus
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
3.4.24.42
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
atrolysin C
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
158886-17-0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Acetyl-Val-Ala-Leu-Leu-Ala + H2O
?
-
best substrate of synthetic acetylated pentapeptides
-
-
-
Angiotensin I + H2O
Asp-Arg-Val-Tyr-Ile-His + Pro + Phe-His-Leu
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu, cleaved at His-Pro and Pro-Phe
-
-
Gelatin of collagen type V + H2O
Hydrolyzed gelatin of collagen type V
-
i.e. denatured collagen, hydrolysis at 38�C and above, not below
MW 130000, MW 118000, MW 93000 and MW 85000 fragments
-
Luteinizing hormone-releasing hormone + H2O
?
-
cleavage sites: Trp3-Ser4, Gly6-Leu7
-
-
-
Met-enkephalin + H2O
Tyr-Gly-Gly + Phe-Met
-
i.e. Tyr-Gly-Gly-Phe-Met, cleavage site: Gly3-Phe4
-
-
-
2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzyl amide + H2O
?
-
-
-
-
-
Basement membrane preparation + H2O
Soluble peptides
-
poor substrate: component band a
-
-
Basement membranes surrounding capillaries + H2O
?
-
involved in disruption of capillary membranes causing hemorrhage in surrounding tissue
-
-
-
Basement membranes surrounding capillaries + H2O
?
-
together with hemorrhagic toxins a, b, e and f responsible for hemorrhage
-
-
-
Basement membranes surrounding capillaries + H2O
?
-
together with atrolysins B and E member of the class P-I hemorrhagic toxins
-
-
-
Basement membranes surrounding capillaries + H2O
?
-
less potent hemorrhagic toxins of Crotalus atrox venom
-
-
-
bovine aggrecan monomer + H2O
?
-
purified atrolysin C can cleave at the cleavage sites VIPEN + FFBVG and ITEGE + ARGSV independently
-
-
?
Collagen type IV + H2O
Hydrolyzed collagen type IV
-
basement membrane component, alpha1 (MW 185000) and alpha2 (MW 170000) chain
-
-
-
Collagen type IV + H2O
Hydrolyzed collagen type IV
-
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
-
Gelatin of collagen type I + H2O
Hydrolyzed gelatin of collagen type I
-
i.e. denatured collagen
-
-
-
Gelatin of collagen type I + H2O
Hydrolyzed gelatin of collagen type I
-
i.e. denatured collagen
MW 60000 and MW 50000 fragments
-
Leu-Val-Glu-Ala-Leu-Tyr-Leu + H2O
Leu-Val-Glu-Ala + Leu-Tyr-Leu
-
cleavage at Ala-Leu
-
-
-
Leu-Val-Glu-Ala-Leu-Tyr-Leu + H2O
Leu-Val-Glu-Ala + Leu-Tyr-Leu
-
peptide derived from insulin B-chain, best substrate
-
-
-
Oxidized insulin B-chain + H2O
?
-
cleavage at His5-Leu6, His10-Leu11, Ala14-Leu15 (most rapidly cleaved bond)
-
-
-
Oxidized insulin B-chain + H2O
?
-
cleaves the same bonds as atrolysin B and A (the latter except Gly23-Phe24)
-
-
-
Oxidized insulin B-chain + H2O
?
-
cleavage at Tyr16-Leu17 (slightly less rapidly cleaved bond)
-
-
-
Oxidized insulin B-chain + H2O
?
-
Crotalus ruber ruber toxin HT-3 does not cleave the His5-Leu6 bond which is cleaved by HT-2
-
-
-
von Willebrand factor + H2O
?
-
VWF is a large, multidomain glycoprotein present in human blood and in the secretory granules of endothelial cells and platelets
-
-
?
von Willebrand factor + H2O
?
-
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
-
-
?
additional information
?
-
-
no hydrolysis of interstitial collagen, native type I collagen
-
-
-
additional information
?
-
-
cleavage specificity, compared to hemorrhagic toxins a and b
-
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
von Willebrand factor + H2O
?
-
VWF is a large, multidomain glycoprotein present in human blood and in the secretory granules of endothelial cells and platelets
-
-
?
Basement membranes surrounding capillaries + H2O
?
-
involved in disruption of capillary membranes causing hemorrhage in surrounding tissue
-
-
-
Basement membranes surrounding capillaries + H2O
?
-
together with hemorrhagic toxins a, b, e and f responsible for hemorrhage
-
-
-
Basement membranes surrounding capillaries + H2O
?
-
together with atrolysins B and E member of the class P-I hemorrhagic toxins
-
-
-
Basement membranes surrounding capillaries + H2O
?
-
less potent hemorrhagic toxins of Crotalus atrox venom
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tissue inhibitor of metalloproteinase 3
-
N-terminal domain of the tissue inhibitor of metalloproteinase 3 is a potent inhibitor
-
1,10-phenanthroline
-
inhibits proteolytic and hemorrhagic activity of atrolysin C
alpha2-Macroglobulin
-
inhibits proteolytic and hemorrhagic activity of atrolysin C
-
phosphoramidon
-
i.e. N-[L-rhamnopyranosyl-oxyhydroxyphosphinyl]-L-leucyl-L-tryptophan, isozyme Ht-c
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
-
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
-
additional information
-
benzamidine, tosyl-L-Phe chloromethyl ketone, soybean or egg white trypsin inhibitor or PCMB
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
ORGANISM
UNIPROT
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24000
additional information
additional information
-
they differ by a single amino acid substitution at position 181, Ala (Cc) or Asp (Cd)
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)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
-
1 * 25000, Crotalus ruber ruber, toxin HT-2; 1 * 25500, Crotalus ruber ruber, toxin HT-3
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
molecular characteristics that influence the toxic effects of snake venom metalloproteases, subdivision in hemorrhagic and non-hemorrhagic snake venom metalloproteases
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 3.4.24.42)
html completed
Use of this online version of BRENDA is free but requires a license. See terms of use.
Information
