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Literature summary extracted from

  • Banks, R.B.; Cooke, R.T.
    Chromate reduction by rabbit liver aldehyde oxidase (1986), Biochem. Biophys. Res. Commun., 137, 8-14.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.3.1 KCN 59% inhibition at 0.2 mM Oryctolagus cuniculus
1.2.3.1 menadione 59% inhibition at 0.2 mM Oryctolagus cuniculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.3.1 Mo5+
-
Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
1.2.3.1 Oryctolagus cuniculus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.3.1 liver
-
Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.3.1 0.006
-
chromate reductase activity Oryctolagus cuniculus
1.2.3.1 0.12
-
ferricyanide reduction Oryctolagus cuniculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.3.1 6-methylpurine + H2O + chromate
-
Oryctolagus cuniculus ?
-
?
1.2.3.1 benzaldehyde + H2O + O2 chromate as electron acceptor Oryctolagus cuniculus benzoic acid + H2O2
-
?
1.2.3.1 N1-methylnicotinamide + H2O + O2 chromate as electron acceptor, reduction of chromate Oryctolagus cuniculus N1-methyl-2-pyridone-5-carboxamide + N1-methyl-4-pyridone-3-carboxamide + H2O2
-
?
1.2.3.1 quinoline + H2O + electron donor chromate as electron donor Oryctolagus cuniculus ?
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.3.1 FAD
-
Oryctolagus cuniculus