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1.14.13.2: 4-hydroxybenzoate 3-monooxygenase

This is an abbreviated version!
For detailed information about 4-hydroxybenzoate 3-monooxygenase, go to the full flat file.

Word Map on EC 1.14.13.2

Reaction

4-hydroxybenzoate
+
NADPH
 +
H+
 +
O2
=
3,4-dihydroxybenzoate
 +
NADP+
 +
H2O

Synonyms

4-HBA 3-hydroxylase, 4-HBA 3-monooxygenase, 4-HBA-3-hydroxylase, 4-HBMO, 4-hydroxybenzoate 3-hydroxylase, 4-hydroxybenzoate 3-monooxygenase, 4-hydroxybenzoate hydroxylase, 4-hydroxybenzoate monooxygenase, 4-hydroxybenzoic hydroxylase, 4HBA 3-hydroxylase, An_PhhA, BxeA2040, FAD-dependent 4-hydroxybenzoate hydroxylase, fungal 4-hydroxybenzoate 3-hydroxylase, HBH, m-hydroxybenzoate hydroxylase, MobA, NADPH-dependent 4-HBA hydroxylase, ncgl1032, oxygenase, 4-hydroxybenzoate 3-mono-, p-hydroxybenzoate hydroxylase, p-hydroxybenzoate-3-hydroxylase, p-hydroxybenzoic acid hydrolase, p-hydroxybenzoic acid hydroxylase, p-hydroxybenzoic hydroxylase, PaPobA, para-hydroxybenzoate hydroxylase, PHBAD, PHBH, PHBHase, PHBHCn2, phhA, PobA, pobACg, POHBase, Reut_B4006

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
                1.14.13.2 4-hydroxybenzoate 3-monooxygenase

Crystallization

Crystallization on EC 1.14.13.2 - 4-hydroxybenzoate 3-monooxygenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion method in the presence of NaH2PO4 and K2HPO4 as precipitants. X-ray diffraction data are collected to a maximum resolution of 2.5 A on a synchrotron beamline. The crystal belongs to the hexagonal space group P6(3)22, with unit-cell parameters a = b = 94.72, c = 359.68 A, gamma = 120°. The asymmetric unit contains two molecules
-
crystal structure of mutant enzyme Y201F, Y385F, and N300D
-
hanging drop vapor diffusion, hanging drops containing 4 mg/ml protein, 100 mM potassium phosphate, pH 7.0, 0.05 mM glutathione, 30 mM sodium sulfite, 0.02 mM FAD, 450 mM ammonium sulfate are equilibrated at 30°C for 7-10 days against a well solution of similar composition, but containing 900 mM ammonium sulfate, crystals of R220Q PHBH diffract to approx. 2.0 A
purifed enzyme mutant Y385F in complex with 3,4-dihydroxybenzoate, X-ray diffraction structure determination and analysis
crystal of the enzyme complexed with 4-hydroxybenzoate are obtained using the hanging-drop method
-
crystal structure of wild-type p-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate, 2,4-dihydroxybenzoate, and 2-hydroxy-4-aminobenzoate and of the Tyr222Ala mutant complexed with 2-hydroxy-4-aminobenzoate
-
crystallization of mutant enzymes H162R and R269T by hanging drop vapour diffusion method
-
crystals of a arabinoflavin adenine dinucleotide -containing 4-hydroxybenzoate hydroxylase in complex with 4-hydroxybenzoate are obtained using the hanging drop method
-
enzyme bound in a crystal is able to convert 4-hydroxybenzoate
-
purified enzyme, sitting drop vapour diffusion method, mixing of 13.8 mg/ml protein in 100 mM Tris-HCl, pH 8.3, 5 mM 2-mercaptoethanol, and 1 mM FAD, with a reservoir solution containing 200 mM potassium thiocyanate, 100 mM bis-Tris propane, pH 6.5, and 20% w/v PEG 3350, in a 1:1 ratio, and equilibration against 0.1 ml of reservoir solution, at 19°C, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement using the structure of wild-type enzyme pHBH from Pseudomonas fluorescens (PDB ID 1pbb) as a search model
structure in complex with FAD. Structural comparison of p-hydroxybenzoate hydroxylase (PobA) from Pseudomonas putida, EC 1.14.13.2, 2-hydroxybiphenyl 3-monooxygenase (HbpA) from Pseudomonas nitroreducens, EC 1.14.13.44, and 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO) from Mesorhizobium japonicum. The portions of the residues required for substrate and FAD binding are identical, including the betaalphabeta fold and beta-sheet wall