1.14.13.113: FAD-dependent urate hydroxylase

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For detailed information about FAD-dependent urate hydroxylase, go to the full flat file.

Reaction

Synonyms

FAD-dependent urate oxidase, flavin adenine dinucleotide-dependent urate oxidase, HpxO, HpxO enzyme, HpyO, urate hydroxylase, XCC0279

ECTree

1 Oxidoreductases

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor

1.14.13.113 FAD-dependent urate hydroxylase

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Results	in table
471	AA Sequence
4	Cloned(Commentary)
8	Cofactor
2	Crystallization (Commentary)
13	kcat/KM [mM/s]
14	KM Value [mM]
3	Molecular Weight [Da]
8	Natural Substrates/ Products (Substrates)
6	Organism
4	Pathway
1	pH Optimum
8	Protein Variants
2	Purification (Commentary)
1	Reaction
1	Reaction Type
6	Reference
9	Substrates and Products (Substrate)
4	Subunits
12	Synonyms
1	Systematic Name
13	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.14.13.113 - FAD-dependent urate hydroxylase

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hanging drop vapor diffusion method, using 0.05 M KH2PO4 and 20% (w/v) PEG 8000

Klebsiella pneumoniae

A6T923

724386

structures of enzyme with and without uric acid at 2.0 and 2.2 A, respectively, and of the R204Q variant at 2.0 A resolution in the absence of uric acid. The variant structure is very similar to that of wild-type HpxO except for the conformation of Arg103, which interacts with FAD in the variant but not in the wild-type structure. The R204Q variant results in the uncoupling of nicotinamide adenine dinucleotide oxidation from uric acid hydroxylation. This suggests that Arg204 facilitates the deprotonation of uric acid, activating it for the oxygen transfer

Klebsiella pneumoniae

A6T923

724386