Literature summary for 1.14.13.7 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
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)

Crystallization (Comment)	Organism
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.

Crystallization (Comment)

Organism

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

Metals/Ions	Comment	Organism	Structure
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

Organism	UniProt	Comment	Textmining
Pseudomonas sp.	-	-	-
Pseudomonas sp. OX1	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
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)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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.	?	-	?
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

Subunits	Comment	Organism
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

Synonyms	Comment	Organism
phenol hydroxylase	-	Pseudomonas sp.
PHH	-	Pseudomonas sp.