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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
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articular
- osteoarthritis
- joint
- chondrocytes
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proteoglycans
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explants
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metalloproteinases
- collagen
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thrombospondin
- glycosaminoglycans
- adamts-4
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disintegrin
- knee
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neoepitope
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interglobular
- synovial
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aggrecanolysis
- chondroitin
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arthritic
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aggrecan-degrading
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timp-3
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versican
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nitege
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chondroprotective
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interleukin-1alpha
- adamalysin
- mannosamine
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disintegrin-like
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matrix-degrading
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svmps
- arthritides
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mmp-mediated
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meniscal
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Specify your search results
The expected taxonomic range for this enzyme is: Crotalus
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EC NUMBER 
COMMENTARY 
3.4.24.42
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RECOMMENDED NAME
GeneOntology No.
atrolysin C
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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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
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CAS REGISTRY NUMBER
COMMENTARY
158886-17-0
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
?
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best substrate of synthetic acetylated pentapeptides
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Angiotensin I + H2O
Asp-Arg-Val-Tyr-Ile-His + Pro + Phe-His-Leu
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i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu, cleaved at His-Pro and Pro-Phe
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Gelatin of collagen type V + H2O
Hydrolyzed gelatin of collagen type V
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i.e. denatured collagen, hydrolysis at 38�C and above, not below
MW 130000, MW 118000, MW 93000 and MW 85000 fragments
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Luteinizing hormone-releasing hormone + H2O
?
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cleavage sites: Trp3-Ser4, Gly6-Leu7
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-
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Met-enkephalin + H2O
Tyr-Gly-Gly + Phe-Met
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i.e. Tyr-Gly-Gly-Phe-Met, cleavage site: Gly3-Phe4
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2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzyl amide + H2O
?
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Basement membrane preparation + H2O
Soluble peptides
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poor substrate: component band a
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Basement membranes surrounding capillaries + H2O
?
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involved in disruption of capillary membranes causing hemorrhage in surrounding tissue
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Basement membranes surrounding capillaries + H2O
?
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together with hemorrhagic toxins a, b, e and f responsible for hemorrhage
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Basement membranes surrounding capillaries + H2O
?
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together with atrolysins B and E member of the class P-I hemorrhagic toxins
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Basement membranes surrounding capillaries + H2O
?
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less potent hemorrhagic toxins of Crotalus atrox venom
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bovine aggrecan monomer + H2O
?
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purified atrolysin C can cleave at the cleavage sites VIPEN + FFBVG and ITEGE + ARGSV independently
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?
Collagen type IV + H2O
Hydrolyzed collagen type IV
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basement membrane component, alpha1 (MW 185000) and alpha2 (MW 170000) chain
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Collagen type IV + H2O
Hydrolyzed collagen type IV
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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
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Gelatin of collagen type I + H2O
Hydrolyzed gelatin of collagen type I
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i.e. denatured collagen
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Gelatin of collagen type I + H2O
Hydrolyzed gelatin of collagen type I
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i.e. denatured collagen
MW 60000 and MW 50000 fragments
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Leu-Val-Glu-Ala-Leu-Tyr-Leu + H2O
Leu-Val-Glu-Ala + Leu-Tyr-Leu
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cleavage at Ala-Leu
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Leu-Val-Glu-Ala-Leu-Tyr-Leu + H2O
Leu-Val-Glu-Ala + Leu-Tyr-Leu
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peptide derived from insulin B-chain, best substrate
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Oxidized insulin B-chain + H2O
?
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cleavage at His5-Leu6, His10-Leu11, Ala14-Leu15 (most rapidly cleaved bond)
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Oxidized insulin B-chain + H2O
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cleaves the same bonds as atrolysin B and A (the latter except Gly23-Phe24)
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Oxidized insulin B-chain + H2O
?
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cleavage at Tyr16-Leu17 (slightly less rapidly cleaved bond)
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Oxidized insulin B-chain + H2O
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Crotalus ruber ruber toxin HT-3 does not cleave the His5-Leu6 bond which is cleaved by HT-2
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von Willebrand factor + H2O
?
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VWF is a large, multidomain glycoprotein present in human blood and in the secretory granules of endothelial cells and platelets
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?
von Willebrand factor + H2O
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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
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?
additional information
?
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no hydrolysis of interstitial collagen, native type I collagen
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additional information
?
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cleavage specificity, compared to hemorrhagic toxins a and b
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additional information
?
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substrate requirements: small aliphatic residues at P1 (Ala or Gly) and Leu at P2
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additional information
?
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substrate digestion patterns differ from those of atrolysins A and E
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additional information
?
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peptides of four residues or less are not hydrolyzed, no significant degradation of fibrin
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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
?
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VWF is a large, multidomain glycoprotein present in human blood and in the secretory granules of endothelial cells and platelets
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-
?
Basement membranes surrounding capillaries + H2O
?
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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
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Basement membranes surrounding capillaries + H2O
?
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less potent hemorrhagic toxins of Crotalus atrox venom
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
additional information
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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
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tissue inhibitor of metalloproteinase 3
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N-terminal domain of the tissue inhibitor of metalloproteinase 3 is a potent inhibitor
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1,10-phenanthroline
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inhibits proteolytic and hemorrhagic activity of atrolysin C
alpha2-Macroglobulin
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inhibits proteolytic and hemorrhagic activity of atrolysin C
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phosphoramidon
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i.e. N-[L-rhamnopyranosyl-oxyhydroxyphosphinyl]-L-leucyl-L-tryptophan, isozyme Ht-c
additional information
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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
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additional information
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tissue inhibitor of metalloproteinase 1 and tissue inhibitor of metalloproteinase 2 have no inhibitory activity
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additional information
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inhibitory protein in the serum of Bothrops jararaca
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additional information
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the isolated recombinant cysteine-rich domain of atrolysin A does not inhibit full-length atrolysin activity, overview
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additional information
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benzamidine, tosyl-L-Phe chloromethyl ketone, soybean or egg white trypsin inhibitor or PCMB
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.31
acetyl-Val-Ala-Leu-Gly-Gly
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isozyme c, acetyl-Val-Ala-Leu-Gly-Ala, 2-aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzyl amide
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24000
additional information
additional information
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they differ by a single amino acid substitution at position 181, Ala (Cc) or Asp (Cd)
additional information
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amino acid composition; isozymes Cc and Cd share identical antigenic structures
additional information
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amino acid composition; they differ by a single amino acid substitution at position 181, Ala (Cc) or Asp (Cd)
additional information
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amino acid composition; amino acid sequence (81% identity of toxins HT-2 and Ht-d)
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
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1 * 25000, Crotalus ruber ruber, toxin HT-2; 1 * 25500, Crotalus ruber ruber, toxin HT-3
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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
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LINKS TO OTHER DATABASES (specific for EC-Number 3.4.24.42)
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