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Information on EC 1.17.9.1 - 4-methylphenol dehydrogenase (hydroxylating) and Organism(s) Pseudomonas putida and UniProt Accession P09788
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1.17.9.1 4-methylphenol dehydrogenase (hydroxylating)IUBMB Comments
This bacterial enzyme contains a flavin (FAD) subunit and a cytochrome c subunit. The flavin subunit abstracts two hydrogen atoms from the substrate, forming a quinone methide intermediate, then hydrates the latter at the benzylic carbon with a hydroxyl group derived from water. The protons are lost to the bulk solvent, while the electrons are passed to the heme on the cytochrome subunit, and from there to azurin, a small copper-binding protein that is co-localized with the enzyme in the periplasm. The first hydroxylation forms 4-hydroxybenzyl alcohol; a second hydroxylation converts this into 4-hydroxybenzaldehyde.
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Word Map
- 1.17.9.1
- putida
-
flavocytochrome
- flavoproteins
- flavin
- p-hydroxybenzaldehyde
-
p-hydroxybenzyl
- azurins
-
vanillyl
-
n.c.i.b
- mendocina
-
ncimb
-
geobacter
-
flavinylation
- metallireducens
-
mcintire
-
alpha2beta2
- 4-ethylphenol
- analysis
The taxonomic range for the selected organisms is: Pseudomonas putida
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
p-cresol methylhydroxylase, p-cresol methylhydroxylase a, para-cresol methylhydroxylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
p-cresol methylhydroxylase
p-cresol methylhydroxylase A
-
2 enzyme forms with various MW and Km are formed during growth on 3,5-xylenol - hydroxylase A - and 4-cresol - hydroxylase B
p-cresol methylhydroxylase B
-
2 enzyme forms with various MW and Km are formed during growth on 3,5-xylenol - formation of hydroxylase A - and on 4-cresol - formation of hydroxylase B
p-cresol-(acceptor) oxidoreductase (hydroxylating)
-
-
-
-
PCMH
additional information
-
consists of a c-type cytochrome subunit PchC and two flavoprotein subunits PchF
p-cresol methylhydroxylase
-
-
-
-
PCMH
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-methylphenol + 4 oxidized azurin + H2O = 4-hydroxybenzaldehyde + 4 reduced azurin + 4 H+
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
4-methylphenol:oxidized azurin oxidoreductase (methyl-hydroxylating)
This bacterial enzyme contains a flavin (FAD) subunit and a cytochrome c subunit. The flavin subunit abstracts two hydrogen atoms from the substrate, forming a quinone methide intermediate, then hydrates the latter at the benzylic carbon with a hydroxyl group derived from water. The protons are lost to the bulk solvent, while the electrons are passed to the heme on the cytochrome subunit, and from there to azurin, a small copper-binding protein that is co-localized with the enzyme in the periplasm. The first hydroxylation forms 4-hydroxybenzyl alcohol; a second hydroxylation converts this into 4-hydroxybenzaldehyde.
CAS REGISTRY NUMBER
COMMENTARY
66772-07-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,4-xylenol + acceptor + H2O
4-hydroxy-3-methylbenzaldehyde + reduced acceptor
-
-
-
-
?
2,4-xylenol + phenazine methosulfate + H2O
4-hydroxy-3-methylbenzaldehyde + reduced phenazine methosulfate + H+
-
-
-
-
?
2-bromo-4-methylphenol + acceptor + H2O
3-bromo-4-hydroxybenzaldehyde + reduced acceptor
-
-
-
-
?
2-methoxy-4-methylphenol + acceptor + H2O
3-methoxy-4-hydroxybenzaldehyde + reduced acceptor
-
-
-
-
?
3,4-dimethylphenol + acceptor + H2O
2-methyl-4-hydroxybenzaldehyde + reduced acceptor
-
-
-
-
?
3-fluoro-4-methylphenol + acceptor + H2O
2-fluoro-4-hydroxybenzaldehyde + reduced acceptor
-
-
-
-
?
4-cresol + azurin + H2O
4-hydroxybenzaldehyde + reduced azurin
-
azurin is the physiological acceptor
-
-
?
4-cresol + phenazine methosulfate + H2O
4-hydroxybenzyl alcohol + reduced phenazine methosulfate
-
-
-
-
?
4-hydroxybenzyl alcohol + acceptor
4-hydroxybenzaldehyde + reduced acceptor
-
-
-
-
?
4-methyl-3-nitrophenol + acceptor + H2O
2-nitro-4-hydroxybenzaldehyde + reduced acceptor
-
-
-
-
?
4-methylcatechol + acceptor + H2O
3,4-dihydroxybenzaldehyde + reduced acceptor
-
-
-
-
?
4-methylphenol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor + H+
-
-
-
-
?
4-methylphenol + phenazine methosulfate + H2O
4-hydroxybenzaldehyde + reduced phenazine methosulfate + H+
-
-
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
via intermediate 4-hydroxybenzylalcohol
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
via intermediate 4-hydroxybenzylalcohol, degradation of toxic 4-cresol
-
-
?
2,4-xylenol + acceptor + H2O
3-methyl-4-hydroxybenzaldehyde + reduced acceptor
-
-
-
-
?
2,4-xylenol + acceptor + H2O
3-methyl-4-hydroxybenzaldehyde + reduced acceptor
-
i.e. 2,4-dimethylphenol
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
-
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
acceptor: phenazine methosulfate
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
acceptor: phenazine methosulfate
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
no activity with 2,6-dichlorophenol-indophenol as acceptor
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
4-hydroxybenzyl alcohol is an enzyme-free intermediate
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
no activity with O2, K3Fe(CN)6 or methylene blue
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
acceptor: azurin
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
acceptor: azurin
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
acceptor: 2,6-dichlorophenol-indophenol
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
the enzyme catalyzes both 4-cresol hydroxylation and further oxidation of the product, 4-hydroxybenzyl alcohol to 4-hydroxybenzaldehyde
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
the enzyme catalyzes both 4-cresol hydroxylation and further oxidation of the product, 4-hydroxybenzyl alcohol to 4-hydroxybenzaldehyde
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
the enzyme catalyzes both 4-cresol hydroxylation and further oxidation of the product, 4-hydroxybenzyl alcohol to 4-hydroxybenzaldehyde
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
the enzyme catalyzes both 4-cresol hydroxylation and further oxidation of the product, 4-hydroxybenzyl alcohol to 4-hydroxybenzaldehyde
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
the enzyme catalyzes both 4-cresol hydroxylation and further oxidation of the product, 4-hydroxybenzyl alcohol to 4-hydroxybenzaldehyde
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
the enzyme catalyzes both 4-cresol hydroxylation and further oxidation of the product, 4-hydroxybenzyl alcohol to 4-hydroxybenzaldehyde
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
degradation of the toxic p-cresol
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
via intermediate 4-hydroxybenzylalcohol
-
-
?
4-ethylphenol + acceptor + H2O
1-(4'-hydroxyphenyl)ethanol + reduced acceptor
-
-
-
-
?
4-ethylphenol + acceptor + H2O
1-(4'-hydroxyphenyl)ethanol + reduced acceptor
-
stereochemistry
65-70% of the (S)-(-)-isomer
?
additional information
?
-
-
no activity with 2,3-xylenol and 2,5-xylenol
-
-
?
additional information
?
-
-
no activity with 4-methyl-2-nitrophenol, 2,4,5-trimethylphenol, 2-chloro-4,5-dimethylphenol, 2,4,6-trimethylphenol, 2,6-dibromo-4-methylphenol, L-tyrosine, 4-hydroxybenzaldehyde 3-cresol
-
-
?
additional information
?
-
-
hydroxylase A is plasmid encoded and is produced constitutively, as long as the plasmid is maintained by growth on 3,5-xylenol. Hydroxylase B is induced by growth on 4-cresol
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
via intermediate 4-hydroxybenzylalcohol, degradation of toxic 4-cresol
-
-
?
2,4-xylenol + acceptor + H2O
4-hydroxy-3-methylbenzaldehyde + reduced acceptor
-
-
-
-
?
4-cresol + azurin + H2O
4-hydroxybenzaldehyde + reduced azurin
-
azurin is the physiological acceptor
-
-
?
4-methylphenol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor + H+
-
-
-
-
?
additional information
?
-
-
hydroxylase A is plasmid encoded and is produced constitutively, as long as the plasmid is maintained by growth on 3,5-xylenol. Hydroxylase B is induced by growth on 4-cresol
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
degradation of the toxic p-cresol
-
-
?
4-cresol + acceptor + H2O
4-hydroxybenzaldehyde + reduced acceptor
-
via intermediate 4-hydroxybenzylalcohol
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8alpha-O-tyrosyl-FAD
-
the covalently bound flavin is 8alpha-O-tyrosyl-FAD
heme
-
wild type enzyme and recombinant enzyme contains covalently bound heme
additional information
-
only traces of activity with 6-Br-FAD, iso-FAD, 5-deaza-FAD, 6-amino-FAD, or 6-hydroxy-FAD as cofactor
-
cytochrome c
-
enzyme has 2 subunits, one is a c-cytochrome and the other a flavoprotein
cytochrome c
-
enzyme contains covalently bound flavin and a type c cytochrome
cytochrome c
-
the cytochrome subunit is necessary for covalent FAD attachment to the flavoprotein subunit
cytochrome c
-
electron-transfer properties of the flavin and heme components
FAD
-
enzyme has 2 subunits, one is a c-cytochrome and the other a flavoprotein
FAD
-
FAD is covalently attached to Tyr384. The mutant Y384F of the flavoprotein subunit displays stoichiometric noncovalent FAD binding
FAD
-
wild type enzyme and recombinant enzyme contains covalently bound FAD
FAD
-
FAD is covalently attached to Tyr384 of the alpha subunit. Covalent flavinylation occurs by a self-catalytic mechanism. The cytochrome subunit is necessary for covalent FAD attachment to the flavoprotein subunit
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
effect of pH-value and ionic strength on KM-value
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
steady-state and stopped-flow kinetic measurements of the primary deuterium isotope effect
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the 9200 Da c-type cytochrome subunit from Pseudomonas putida NCIMB 9869, overexpressed in recombinant form in Pseudomonas aeruginosa PAO1-LAC
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
using a gene-knockout it is shown that PCMH-encoding gene pchF is necessary for the catabolism of 2,4-xylenol
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58700
alpha2beta2, 2 * 58700 + 2 * 9200, c-type cytochrome subunit PchC (beta) and two flavoprotein subunits PchF (alpha)
9200
alpha2beta2, 2 * 58700 + 2 * 9200, c-type cytochrome subunit PchC (beta) and two flavoprotein subunits PchF (alpha)
10000
-
alpha, beta, 2 * 58000 + 2 * 10000, c-type cytochrome subunit PchC (beta) and two flavoprotein subunits PchF (alpha)
48600
-
alpha2beta2, 2 * 8780 + 2 * 48600, 8780 Da cytochrome subunit and 48600 Da flavoprotein subunit, amino acid analysis
49000
-
alpha2,beta2, 2 * 8500 + 2 * 49000, 95000 Da cytochrome subunit and 49000 Da flavoprotein subunit, amino acid analysis
56000
58000
58700
-
alpha, beta, 2 * 58700 + 2 * 9200, c-type cytochrome subunit PchC (beta) and two flavoprotein subunits PchF (alpha)
59500
-
alpha, beta, 2 * 59500 + 2 * 9200, c-type cytochrome subunit PchC (beta) and two flavoprotein subunits PchF (alpha)
8500
-
alpha2,beta2, 2 * 8500 + 2 * 49000, 95000 Da cytochrome subunit and 49000 Da flavoprotein subunit, amino acid analysis
8780
-
alpha2beta2, 2 * 8780 + 2 * 48600, 8780 Da cytochrome subunit and 48600 Da flavoprotein subunit, amino acid analysis
9200
56000
-
2 * 56000, one subunit is a c-cytochrome and the other a flavoprotein, SDS-PAGE after incubation with SDS and mercaptoethanol
56000
-
2 * 56000, hydroxylase B, SDS-PAGE after incubation with mercaptoethanol
58000
-
2 * 58000, hydroxylase A, SDS-PAGE after incubation with mercaptoethanol
58000
-
alpha, beta, 2 * 58000 + 2 * 10000, c-type cytochrome subunit PchC (beta) and two flavoprotein subunits PchF (alpha)
9200
-
alpha, beta, 2 * 58700 + 2 * 9200, c-type cytochrome subunit PchC (beta) and two flavoprotein subunits PchF (alpha)
9200
-
alpha, beta, 2 * 59500 + 2 * 9200, c-type cytochrome subunit PchC (beta) and two flavoprotein subunits PchF (alpha)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
alpha2beta2, 2 * 58700 + 2 * 9200, c-type cytochrome subunit PchC (beta) and two flavoprotein subunits PchF (alpha)
dimer
tetramer
additional information
-
the subunit dissociation is strongly dependent on ionic strength in the oxidized form of the enzyme but not in the reduced form
dimer
-
2 * 56000, one subunit is a c-cytochrome and the other a flavoprotein, SDS-PAGE after incubation with SDS and mercaptoethanol
dimer
-
2 * 58000, hydroxylase A, SDS-PAGE after incubation with mercaptoethanol
dimer
-
2 * 56000, hydroxylase B, SDS-PAGE after incubation with mercaptoethanol
tetramer
-
alpha2,beta2, 2 * 8500 + 2 * 49000, 95000 Da cytochrome subunit and 49000 Da flavoprotein subunit, amino acid analysis
tetramer
-
alpha2beta2, 2 * 8780 + 2 * 48600, 8780 Da cytochrome subunit and 48600 Da flavoprotein subunit, amino acid analysis
tetramer
-
alpha, beta, 2 * 58000 + 2 * 10000, c-type cytochrome subunit PchC (beta) and two flavoprotein subunits PchF (alpha)
tetramer
-
alpha, beta, 2 * 58700 + 2 * 9200, c-type cytochrome subunit PchC (beta) and two flavoprotein subunits PchF (alpha)
tetramer
-
alpha, beta, 2 * 59500 + 2 * 9200, c-type cytochrome subunit PchC (beta) and two flavoprotein subunits PchF (alpha)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme and alpha subunit, sitting drop vapor diffusion method
crystals prepared by free interface diffusion method in 8% polyethylene glycol 8000
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
apo-PchF[Y384F]
-
the mutant Y384F of the flavoprotein subunit displays stoichiometric noncovalent FAD binding. The mutant flavoprotein subunit associates with the cytochrome subunit, although not as avidly as the wild-type flavoprotein subunit containing covalently bound FAD
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the 9200 Da c-type cytochrome subunit from Pseudomonas putida NCIMB 9869, overexpressed in recombinant form in Pseudomonas aeruginosa PAO1-LAC
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the flavoprotein subunit with non-covalently attached FAD in Escherichia coli
-
the 9200 Da c-type cytochrome subunit from Pseudomonas putida NCIMB 9869 is overexpressed in recombinant form in Pseudomonas aeruginosa PAO1-LAC. Efforts to produce the cytochrome in Escherichia coli using a pET vector, with or without its signal peptide, are unsuccessful, yielding relatively low levels of the protein
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hopper, D.J.; Taylor, D.G.
The purification and properties of p-cresol-(acceptor) oxidoreductase (hydroxylating), a flavocytochrome from Pseudomonas putida
Biochem. J.
167
155-162
1977
Pseudomonas putida
Hopper, D.J.
Incorporation of [18O]water in the formation of p-hydroxybenzyl alcohol by the p-cresol methylhydroxylase from Pseudomonas putida
Biochem. J.
175
345-347
1978
Pseudomonas putida
McIntire, W.; Edmondson, D.E.; Singer, T.P.; Hopper, D.J.
8 alpha-O-Tyrosyl-FAD: a new form of covalently bound flavin from p-cresol methylhydroxylase
J. Biol. Chem.
255
6553-6555
1980
Pseudomonas putida
McIntire, W.; Edmondson, D.E.; Hopper, D.J.; Singer, T.P.
8 alpha-(O-Tyrosyl)flavin adenine dinucleotide, the prosthetic group of bacterial p-cresol methylhydroxylase
Biochemistry
20
3068-3075
1981
Pseudomonas putida
Hopper, D.J.
Redox potential of the cytochrome c in the flavocytochrome p-cresol methylhydroxylase
FEBS Lett.
161
100-102
1983
Comamonas testosteroni, Comamonas testosteroni NCIB 8955, Pseudomonas alcaligenes, Pseudomonas alcaligenes NCIB 9867, Pseudomonas putida, Pseudomonas putida NCIB 9866, Pseudomonas putida NCIB 9869
Causer, M.J.; Hopper, D.J.; McIntire, W.S.; Singer, T.P.
Azurin from Pseudomonas putida: an electron acceptor for p-cresol methylhydroxylase
Biochem. Soc. Trans.
12
1131-1132
1984
Pseudomonas putida, Pseudomonas putida NCIB 9869
-
McIntire, W.; Hopper, D.J.; Craig, J.C.; Everhart, E.T.; Webster, R.V.; Causer, M.J.; Singer, T.P.
Stereochemistry of 1-(4-hydroxyphenyl)ethanol produced by hydroxylation of 4-ethylphenol by p-cresol methylhydroxylase
Biochem. J.
224
617-621
1984
Pseudomonas putida
Hopper, D.J.; Jones, M.R.; Causer, M.J.
Periplasmic location of p-cresol methylhydroxylase in Pseudomonas putida
FEBS Lett.
182
485-488
1985
Pseudomonas putida
Bhattacharyya, A.; Tollin, G.; McIntire, W.; Singer, T.P.
Laser-flash-photolysis studies of p-cresol methylhydroxylase. Electron-transfer properties of the flavin and haem components
Biochem. J.
228
337-345
1985
Pseudomonas putida
Shamala, N.; Lim, L.W.; Mathews, F.S.
Preliminary X-ray study of p-cresol methylhydroxylase (flavocytochrome c) from Pseudomonas putida N.C.I.B. 9869
J. Mol. Biol.
183
517-518
1985
Pseudomonas putida
McIntire, W.; Hopper, D.J.; Singer, T.P.
p-Cresol methylhydroxylase. assay and general properties
Biochem. J.
228
325-335
1985
Pseudomonas putida
Koerber, S.C.; McIntire, W.; Bohmont, C.; Singer, T.P.
Resolution of the flavocytochrome p-cresol methylhydroxylase into subunits and reconstitution of the enzyme
Biochemistry
24
5276-5280
1985
Pseudomonas putida
Kim, J.; Fuller, J.H.; Cecchini, G.; McIntire, W.S.
Cloning, sequencing, and expression of the structural genes for the cytochrome and flavoprotein subunits of p-cresol methylhydroxylase from two strains of Pseudomonas putida
J. Bacteriol.
176
6349-6361
1994
Pseudomonas putida, Pseudomonas putida NCIB 9866, Pseudomonas putida NCIB 9869
Shamala, N.; Lim, L.W.; Mathews, F.S.; McIntire, W.; Singer, T.P.; Hopper, D.J.
Structure of an intermolecular electron-transfer complex: p-cresol methylhydroxylase at 6.0-A resolution
Proc. Natl. Acad. Sci. USA
83
4626-4630
1986
Pseudomonas putida
McIntire, W.; Singer, T.P.; Smith, A.J.; Mathews, F.S.
Amino acid and sequence analysis of the cytochrome and flavoprotein subunits of p-cresol methylhydroxylase
Biochemistry
25
5975-5981
1986
Pseudomonas putida
McIntire, W.S.; Hopper, D.J.; Singer, T.P.
Steady-state and stopped-flow kinetic measurements of the primary deuterium isotope effect in the reaction catalyzed by p-cresol methylhydroxylase
Biochemistry
26
4107-4117
1987
Pseudomonas putida, Pseudomonas putida NCIB 9869
Keat, M.J.; Hopper, D.J.
p-Cresol and 3,5-xylenol methylhydroxylases in Pseudomonas putida N.C.I.B. 9896
Biochem. J.
175
649-658
1978
Pseudomonas putida, Pseudomonas putida NCIB 9869
Cunane, L.M.; Chen, Z.W.; Shamala, N.; Mathews, F.S.; Cronin, C.N.; McIntire, W.S.
Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: Gated substrate entry and proton relays support the proposed catalytic mechanism
J. Mol. Biol.
295
357-374
2000
Pseudomonas putida
Engst, S.; Kuusk, V.; Efimov, I.; Cronin, C.N.; McIntire, W.S.
Properties of p-cresol methylhydroxylase flavoprotein overproduced by Escherichia coli
Biochemistry
38
16620-16628
1999
Pseudomonas putida
Kim, J.; Fuller, J.H.; Kuusk, V.; Cunane, L.; Chen, Z.; Mathews, F.S.; McIntire, W.S.
The cytochrome subunit is necessary for covalent FAD attachment to the flavoprotein subunit of p-cresol methylhydroxylase
J. Biol. Chem.
270
31202-31209
1995
Pseudomonas putida
Efimov, I.; Cronin, C.N.; McIntire, W.S.
Effects of noncovalent and covalent FAD binding on the redox and catalytic properties of p-cresol methylhydroxylase
Biochemistry
40
2155-2166
2001
Pseudomonas putida
Cronin, C.N.; McIntire, W.S.
Heterologous expression in Pseudomonas aeruginosa and purification of the 9.2-kDa c-type cytochrome subunit of p-cresol methylhydroxylase
Protein Expr. Purif.
19
74-83
2000
Pseudomonas putida
Efimov, I.; McIntire, W.S.
A study of the spectral and redox properties and covalent flavinylation of the flavoprotein component of p-cresol methylhydroxylase reconstituted with FAD analogues
Biochemistry
43
10532-10546
2004
Pseudomonas putida
Efimov, I.; Cronin, C.N.; Bergmann, D.J.; Kuusk, V.; McIntire, W.S.
Insight into covalent flavinylation and catalysis from redox, spectral, and kinetic analyses of the R474K mutant of the flavoprotein subunit of p-cresol methylhydroxylase
Biochemistry
43
6138-6148
2004
Pseudomonas putida, Pseudomonas putida NCIMB 9869
Cunane, L.M.; Chen, Z.W.; McIntire, W.S.; Mathews, F.S.
p-Cresol methylhydroxylase: alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit
Biochemistry
44
2963-2973
2005
Pseudomonas putida (P09788)
Efimov, I.; McIntire, W.S.
Relationship between charge-transfer interactions, redox potentials, and catalysis for different forms of the flavoprotein component of p-cresol methylhydroxylase
J. Am. Chem. Soc.
127
732-741
2005
Pseudomonas putida
Chen, Y.F.; Chao, H.; Zhou, N.Y.
The catabolism of 2,4-xylenol and p-cresol share the enzymes for the oxidation of para-methyl group in Pseudomonas putida NCIMB 9866
Appl. Microbiol. Biotechnol.
98
1349-1356
2014
Pseudomonas putida
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