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Literature summary for 1.4.3.2 extracted from
- Characterization of L-amino acid oxidase derived from Crotalus adamanteus venom procoagulant and anticoagulant activities (2019), Int. J. Mol. Sci., 20, 4853 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| PMSF | exposure of the enzyme to phenylmethylsulfonyl fluoride results in the LAAO expressing anticoagulant activity, preventing contact activation generated thrombin from forming a clot | Crotalus adamanteus |  |
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | enzyme displays fibrinogen polymerizing procoagulation and PMSF-associated anticoagulation. The LAAO must be polymerizing fibrinogen independent of endogenous thrombin generation and FXIII crosslinking. The direct deaminating action of LAAO, not the coincident generation of H2O2, is responsible for the coagulation procoagulant profile | Crotalus adamanteus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | LAAO is not inhibited by carbon monoxide releasing molecule CORM-2 nor by EDTA | Crotalus adamanteus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Crotalus adamanteus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Crotalus adamanteus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| venom | - |
Crotalus adamanteus | - |
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