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Literature summary for 3.4.24.1 extracted from

  • Suntravat, M.; Langlais, P.R.; Sanchez, E.E.; Nielsen, V.G.
    CatroxMP-II a heme-modulated fibrinogenolytic metalloproteinase isolated from Crotalus atrox venom (2018), Biometals, 31, 585-593 .
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
CORM-2 a tricarbonyldichlororuthenium (II) dimer, and a CO releasing molecule, inhibits the fibrinogenolytic effects of CatroxMP-II on coagulation kinetics in human plasma via CO Crotalus atrox
EDTA complete einhibition at 0.1 mM Crotalus atrox
additional information no inhibition by PMSF Crotalus atrox

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular venom Crotalus atrox
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a metal-dependent a P-II class metalloproteinase from venom Crotalus atrox

Organism

Organism UniProt Comment Textmining
Crotalus atrox P34182
-
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
Crotalus atrox
-

Subunits

Subunits Comment Organism
? x * 21000, SDS-PAGE Crotalus atrox
More trypsin peptide mapping and mass spectrometric analysis Crotalus atrox

Synonyms

Synonyms Comment Organism
atrolysin-e
-
Crotalus atrox
CatroxMP-II
-
Crotalus atrox
fibrinogenolytic metalloproteinase
-
Crotalus atrox
snake venom metalloproteinase
-
Crotalus atrox
SVMP
-
Crotalus atrox

General Information

General Information Comment Organism
metabolism the enzyme is regulated by heme Crotalus atrox
additional information the snake venom metalloproteinase is heme-bound and CO-inhibited Crotalus atrox