FAD-dependent urate hydroxylase - définition. Qu'est-ce que FAD-dependent urate hydroxylase
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Qu'est-ce (qui) est FAD-dependent urate hydroxylase - définition


FAD-dependent urate hydroxylase         
CLASS OF ENZYMES
EC 1.14.13.113; HpxO enzyme; FAD-dependent urate oxidase; Urate hydroxylase; Urate,NADH:oxygen oxidoreductase (5-hydroxyisourate forming); Urate,NADH:oxygen oxidoreductase; TRNA-5,6-dihydrouracil16 17:NAD(P)+ oxidoreductase
FAD-dependent urate hydroxylase (, HpxO enzyme, FAD-dependent urate oxidase, urate hydroxylase) is an enzyme with systematic name urate,NADH:oxygen oxidoreductase (5-hydroxyisourate forming).
Tyrosine hydroxylase         
  • Tyrosine hydroxylase catalyzes the rate limiting step in [[catecholamine]] biosynthesis
  • substrate]] would enter from.
MAMMALIAN PROTEIN FOUND IN HOMO SAPIENS
Tyrosine 3-monooxygenase; Tyrosine hydroxylase inhibitor; Tyrosine-3-hydroxylase; EC 1.14.16.2; Tyrosine 3-hydroxylase; L-tyrosine,tetrahydrobiopterin:oxygen oxidoreductase (3-hydroxylating)
Tyrosine hydroxylase or tyrosine 3-monooxygenase is the enzyme responsible for catalyzing the conversion of the amino acid L-tyrosine to L-3,4-dihydroxyphenylalanine (L-DOPA). It does so using molecular oxygen (O2), as well as iron (Fe2+) and tetrahydrobiopterin as cofactors.
Alpha-ketoglutarate-dependent hydroxylases         
  • Common inhibitors of αKG-dependent dioxygenases. They compete against the cosubstrate αKG for binding to the active site Fe(II).
  • Consensus catalytic mechanism of the αKG-dependent dioxygenase superfamily.
  • prolyl hydroxylase isoform 2]] (PHD2), a human αKG-dependent dioxygenase. The Fe(II) is coordinated by two imidazoles and one carboxylate provided by the protein.  Other ligands on iron, which are transiently occupied αKG and O<sub>2</sub>, are omitted for clarity.
CLASS OF ENZYMES
2-oxoglutarate (2OG)-dependent dioxygenases; Alpha-ketoglutarate-dependent hydroxylase; 2-oxoglutarate–dependent dioxygenase; 2-oxoglutarate-dependent dioxygenase
Alpha-ketoglutarate-dependent hydroxylases are a major class of non-heme iron proteins that catalyse a wide range of reactions. These reactions include hydroxylation reactions, demethylations, ring expansions, ring closures, and desaturations.