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Literature summary for 3.4.24.1 extracted from

  • Williams, H.F.; Mellows, B.A.; Mitchell, R.; Sfyri, P.; Layfield, H.J.; Salamah, M.; Vaiyapuri, R.; Collins-Hooper, H.; Bicknell, A.B.; Matsakas, A.; Patel, K.; Vaiyapuri, S.
    Mechanisms underpinning the permanent muscle damage induced by snake venom metalloprotease (2019), PLoS Negl. Trop. Dis., 13, e0007041 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.1

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Crotalus atrox
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Collagen + H2O Crotalus atrox
-
 ?
-
 ?
fibrinogen + H2O Crotalus atrox
-
 fibrin + ?
-
 ?

Organism

Organism UniProt Comment Textmining
Crotalus atrox
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme from venom by anion exchange chromatography and gel filtration Crotalus atrox

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
 Crotalus atrox
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Collagen + H2O
-
 Crotalus atrox ?
-
 ?
fibrinogen + H2O
-
 Crotalus atrox fibrin + ?
-
 ?
fibrinogen + H2O from human plasma Crotalus atrox fibrin + ?
-
 ?
Nalpha-benzoyl-L-arginine-7-amido-4-methylcoumarin + H2O
-
 Crotalus atrox Nalpha-benzoyl-L-arginine + 7-amino-4-methylcoumarin
-
 ?

Subunits

Subunits Comment Organism
? x * 50000, SDS-PAGE Crotalus atrox

Synonyms

Synonyms Comment Organism
CAMP
-
 Crotalus atrox
crotalus atrox metalloproteinase
-
 Crotalus atrox
snake venom metalloprotease
-
 Crotalus atrox
SVMP
-
 Crotalus atrox

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Crotalus atrox

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Crotalus atrox

General Information

General Information Comment Organism
evolution the Crotalus atrox metalloproteinase (CAMP) is a group III metalloprotease showing high similarity to VAP2A Crotalus atrox
physiological function snake venom metalloproteases (SVMPs) are a predominant component of viper venoms, and are involved in the degradation of basement membrane proteins (particularly collagen) surrounding the tissues around the bite site. Crotalus atrox metalloprotease (CAMP) displays both collagenolytic and fibrinogenolytic activities and inhibits CRP-XL-induced platelet aggregation. Permanent muscle damage induced by snake venom metalloprotease on tibialis anterior muscle of C57BL/6 mice, mechanism, overview. CAMP significantly damages skeletal muscles by attacking the collagen scaffold and other important basement membrane proteins, and prevents their regeneration through disrupting the functions of satellite cells. CAMP extensively damages the extracellular matrix surrounding the myofibres Crotalus atrox