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Literature summary extracted from

  • Conrads, T.; Hemann, C.; George, G.N.; Pickering, I.J.; Prince, R.C.; Hille, R.
    The active site of arsenite oxidase from Alcaligenes faecalis (2002), J. Am. Chem. Soc., 124, 11276-11277.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.20.99.1 Molybdenum molybdenum enzyme containing inequivalent P- and Q-pterins coordinated to the metal ion, structure analysis Alcaligenes faecalis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.20.99.1 arsenite + azurin + H2O Alcaligenes faecalis
-
arsenate + reduced azurin
-
?
1.20.99.1 arsenite + cytochrome c + H2O Alcaligenes faecalis
-
arsenate + reduced cytochrome c
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.20.99.1 Alcaligenes faecalis
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.20.99.1 arsenite + acceptor + H2O = arsenate + reduced acceptor active site structure Alcaligenes faecalis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.20.99.1 arsenite + azurin + H2O
-
Alcaligenes faecalis arsenate + reduced azurin
-
?
1.20.99.1 arsenite + cytochrome c + H2O
-
Alcaligenes faecalis arsenate + reduced cytochrome c
-
?

Subunits

EC Number Subunits Comment Organism
1.20.99.1 More crystal structure and active site structure analysis Alcaligenes faecalis

Synonyms

EC Number Synonyms Comment Organism
1.20.99.1 arsenite oxidase
-
Alcaligenes faecalis
1.20.99.1 More enzyme is a member of the DMSO-reductase class of molybdenum enzymes Alcaligenes faecalis

Cofactor

EC Number Cofactor Comment Organism Structure
1.20.99.1 pterin inequivalent P- and Q-pterins coordinated to the molybdenum ion, structure analysis Alcaligenes faecalis