Literature summary for 1.14.13.2 extracted from

van Berkel, W.J.H.; Eppink, M.H.M.; Schreuder, H.A.
Crystal structure of p-hydroxybenzoate hydroxylase reconstituted with the modified FAD present in alcohol oxidase from methylotrophic yeasts: evidence for an arabinoflavin (1994), Protein Sci., 3, 2245-2253.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystals of a arabinoflavin adenine dinucleotide -containing 4-hydroxybenzoate hydroxylase in complex with 4-hydroxybenzoate are obtained using the hanging drop method	Pseudomonas fluorescens

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas fluorescens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinat enzyme, cloned in Escherichia coli	Pseudomonas fluorescens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4-hydroxybenzoate + NADPH + O2	-	Pseudomonas fluorescens	protocatechuate + NADP+ + H2O	-	?

Cofactor

Cofactor	Comment	Organism	Structure
arabinoflavin adenine dinucleotide	like native enzyme the arabinoflavin adenine dinucleotide containing 4-hydroxybenzoate hydroxylase preferentially binds the phenolate form of the substrate. The oxidative part of the catalytic cycle of a FAD-containing 4-hydroxybenzoate hydroxylase differs from the native enzyme. Partial uncoupling of hydroxylation results in the formation of about 0.3 mol of 3,4-dihydroxybenzoate and 0.7 mol of H2O2 per mol of NADPH oxidized	Pseudomonas fluorescens
FAD	flavin motion in 4-hydroxybenzoate hydroxylase is important for efficient reduction	Pseudomonas fluorescens

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Release 2023.1 (January 2023)