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Literature summary for 1.2.3.1 extracted from

  • Ferreira, P.; Cerqueira, N.; Fernandes, P.; Romao, M.; Ramos, M.
    Catalytic Mechanism of human aldehyde oxidase (2020), ACS Catal., 10, 9276-9286 .
No PubMed abstract available
Search for more literature for 1.2.3.1

Organism

Organism UniProt Comment Textmining
Homo sapiens Q06278
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phthalazine + H2O + O2
-
 Homo sapiens 1-phthalazinone + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
AOX1
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
molybdenum cofactor during the displacement of the products away from the Moco, the transfer of electrons from the catalytic site to the FAD site is proton-coupled. The most favorable and fastest pathway for the enzyme to complete its catalytic cycle is that with MoV and a deprotonated SH ligand of the Moco with the FAD molecule converted to its semiquinone form, FADH radical Homo sapiens

General Information

General Information Comment Organism
metabolism the oxidation of phthalazine reaction involves three sequential steps: protonation of the substrate's N2 atom by Lys893, nucleophilic attack of the hydroxyl group of the molybdenum cofactor (Moco) to the substrate, and hydride transfer from the substrate to the sulfur atom of the Moco. The rate-limiting step corresponds to hydride transfer. Residue Lys893 plays a relevant role in the reaction, being important for the anchorage of the substrate close to the Moco, and also in the catalytic reaction. During the displacement of the products away from the Moco, the transfer of electrons from the catalytic site to the FAD site is proton-coupled. The most favorable and fastest pathway for the enzyme to complete its catalytic cycle is that with MoV and a deprotonated SH ligand of the Moco with the FAD molecule converted to its semiquinone form, FADH radical Homo sapiens