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Literature summary extracted from

  • Sazinsky, M.H.; Dunten, P.W.; McCormick, M.S.; Didonato, A.; Lippard, S.J.
    X-ray structure of a hydroxylase-regulatory protein complex from a hydrocarbon-oxidizing multicomponent monooxygenase, Pseudomonas sp. OX1 phenol hydroxylase (2006), Biochemistry, 45, 15392-15404.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.7 co-expression of phenol hydroxylase with the regulatory protein in Escherichia coli JM109, expression of selenomethionine-enzyme in Escherichia coli strain BL21(DE3) Pseudomonas sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.13.7 native and SeMet forms of the phenol hydroxylase in complex with its regulatory protein, hanging drop vapor diffusion method, 20°C, 0.035 mM enzyme in 10 mM MES, pH 7.1, and 10% glycerol is mixed with an equal volume of crystallization buffer containing 100 mM Tris, pH 7.0, 150 mM Na2MoO4, 5% glycerol, and 17-20% PEG 8000 (w/w), X-ray diffraction structure determination and analysis at 2.3 Å resolution, molecular replacement, Single-wavelength anomalous dispersion data for the selenomethionine derivative Pseudomonas sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.7 Fe2+ the enzyme contains dinuclear iron active site, structure with a Fe(II)Fe(III) oxidation state, helix E comprises part of the iron-coordinating four-helix bundle Pseudomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.7 Pseudomonas sp.
-
-
-
1.14.13.7 Pseudomonas sp. OX1
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.13.7 phenol + NADPH + H+ + O2 = catechol + NADP+ + H2O catalytic mechanism, conformational changes upon binding of the regulatory protein comonent and effects on catalytic activity Pseudomonas sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.7 additional information the enzyme is a hydrocarbon-oxidizing multicomponent monooxygenase, important for activity is formation of a complex between the hydroxylase and a regulatory protein component Pseudomonas sp. ?
-
 ?
1.14.13.7 additional information the enzyme is a hydrocarbon-oxidizing multicomponent monooxygenase, important for activity is formation of a complex between the hydroxylase and a regulatory protein component Pseudomonas sp. OX1 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.13.7 More the regulatory protein component binds in a canyon on one side of the (alpha,beta)2 enzyme dimer, contacting alpha-subunit helices A, E, and F about 12 A above the diiron core Pseudomonas sp.

Synonyms

EC Number Synonyms Comment Organism
1.14.13.7 phenol hydroxylase
-
 Pseudomonas sp.
1.14.13.7 PHH
-
 Pseudomonas sp.