Anthraniloyl-CoA monooxygenase

anthraniloyl-CoA monooxygenase
Identifiers
EC number 1.14.13.40
CAS number 112692-57-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

In enzymology, an anthraniloyl-CoA monooxygenase (EC 1.14.13.40) is an enzyme that catalyzes the chemical reaction

2-aminobenzoyl-CoA + 2 NAD(P)H + 2 H+ + O2 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+

The 5 substrates of this enzyme are 2-aminobenzoyl-CoA, NADH, NADPH, H+, and O2, whereas its 4 products are 2-amino-5-oxocyclohex-1-enecarboxyl-CoA, H2O, NAD+, and NADP+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 2-aminobenzoyl-CoA,NAD(P)H:oxygen oxidoreductase (de-aromatizing). Other names in common use include anthraniloyl coenzyme A reductase, and 2-aminobenzoyl-CoA monooxygenase/reductase. This enzyme participates in carbazole degradation. It employs one cofactor, FAD.

References

    • Buder R, Fuchs G (1989). "2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme. Purification and some properties of the enzyme". Eur. J. Biochem. 185 (3): 629&ndash, 35. doi:10.1111/j.1432-1033.1989.tb15159.x. PMID 2591379.
    • Buder R, Ziegler K, Fuchs G, Langkau B, Ghisla S (1989). "2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme. Studies on the stoichiometry and the course of the reaction". Eur. J. Biochem. 185 (3): 637&ndash, 43. doi:10.1111/j.1432-1033.1989.tb15160.x. PMID 2591380.
    • Langkau B, Ghisla S, Buder R, Ziegler K, Fuchs G (1990). "2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme. Identification of the reaction products". Eur. J. Biochem. 191 (2): 365&ndash, 71. doi:10.1111/j.1432-1033.1990.tb19131.x. PMID 2384085.
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