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Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.13.2 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

EC Number Organism UniProt Comment Textmining
1.14.13.2 Pseudomonas fluorescens
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.2 4-hydroxybenzoate + NADPH + O2
-
Pseudomonas fluorescens protocatechuate + NADP+ + H2O
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.2 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
1.14.13.2 FAD flavin motion in 4-hydroxybenzoate hydroxylase is important for efficient reduction Pseudomonas fluorescens