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* Residue conservation analysis
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Enzyme class:
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E.C.1.14.13.7
- Phenol 2-monooxygenase.
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Reaction:
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Phenol + NADPH + O2 = catechol + NADP+ + H2O
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Phenol
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+
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NADPH
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+
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O(2)
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=
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catechol
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+
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NADP(+)
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+
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H(2)O
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Cofactor:
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FAD
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FAD
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Gene Ontology (GO) functional annotation
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Biological process
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oxidation-reduction process
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3 terms
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Biochemical function
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oxidoreductase activity
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3 terms
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DOI no:
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Biochemistry
36:495-504
(1997)
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PubMed id:
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Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy.
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H.Qian,
U.Edlund,
J.Powlowski,
V.Shingler,
I.Sethson.
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ABSTRACT
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Phenol hydroxylase from Pseudomonas sp. CF600 is a member of a family of
binuclear iron-center-containing multicomponent oxygenases, which catalyzes the
conversion of phenol and some of its methyl-substituted derivatives to catechol.
In addition to a reductase component which transfers electrons from NADH,
optimal turnover of the hydroxylase requires P2, a protein containing 90 amino
acids which is readily resolved from the other components. The three-dimensional
solution structure of P2 has been solved by 3D heteronuclear NMR spectroscopy.
On the basis of 1206 experimental constraints, including 1060 distance
constraints obtained from NOEs, 70 phi dihedral angle constraints, 42 psi
dihedral angle constraints, and 34 hydrogen bond constraints, a total of 12
converged structures were obtained. The atomic root mean square deviation for
the 12 converged structure with respect to the mean coordinates is 2.48 A for
the backbone atoms and 3.85 A for all the heavy atoms. This relatively large
uncertainty can be ascribed to conformational flexibility and exchange. The
molecular structure of P2 is composed of three helices, six antiparallel
beta-strands, one beta-hairpin, and some less ordered regions. This is the first
structure among the known multicomponent oxygenases. On the basis of the
three-dimensional structure of P2, sequence comparisons with similar proteins
from other multicomponent oxygenases suggested that all of these proteins may
have a conserved structure in the core regions.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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V.Champreda,
Y.J.Choi,
N.Y.Zhou,
and
D.J.Leak
(2006).
Alteration of the stereo- and regioselectivity of alkene monooxygenase based on coupling protein interactions.
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Appl Microbiol Biotechnol, 71,
840-847.
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A.M.Orville,
J.M.Studts,
G.T.Lountos,
K.H.Mitchell,
and
B.G.Fox
(2003).
Crystallization and preliminary analysis of native and N-terminal truncated isoforms of toluene-4-monooxygenase catalytic effector protein.
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Acta Crystallogr D Biol Crystallogr, 59,
572-575.
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E.Griva,
E.Pessione,
S.Divari,
F.Valetti,
M.Cavaletto,
G.L.Rossi,
and
C.Giunta
(2003).
Phenol hydroxylase from Acinetobacter radioresistens S13. Isolation and characterization of the regulatory component.
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Eur J Biochem, 270,
1434-1440.
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J.G.Leahy,
P.J.Batchelor,
and
S.M.Morcomb
(2003).
Evolution of the soluble diiron monooxygenases.
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FEMS Microbiol Rev, 27,
449-479.
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S.Divari,
F.Valetti,
P.Caposio,
E.Pessione,
M.Cavaletto,
E.Griva,
G.Gribaudo,
G.Gilardi,
and
C.Giunta
(2003).
The oxygenase component of phenol hydroxylase from Acinetobacter radioresistens S13.
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Eur J Biochem, 270,
2244-2253.
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E.Cadieux,
V.Vrajmasu,
C.Achim,
J.Powlowski,
and
E.Münck
(2002).
Biochemical, Mössbauer, and EPR studies of the diiron cluster of phenol hydroxylase from Pseudomonas sp. strain CF 600.
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Biochemistry, 41,
10680-10691.
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K.H.Mitchell,
J.M.Studts,
and
B.G.Fox
(2002).
Combined participation of hydroxylase active site residues and effector protein binding in a para to ortho modulation of toluene 4-monooxygenase regiospecificity.
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Biochemistry, 41,
3176-3188.
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B.J.Wallar,
and
J.D.Lipscomb
(2001).
Methane monooxygenase component B mutants alter the kinetics of steps throughout the catalytic cycle.
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Biochemistry, 40,
2220-2233.
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E.Díaz,
A.Ferrández,
M.A.Prieto,
and
J.L.García
(2001).
Biodegradation of aromatic compounds by Escherichia coli.
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Microbiol Mol Biol Rev, 65,
523.
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H.Hemmi,
J.M.Studts,
Y.K.Chae,
J.Song,
J.L.Markley,
and
B.G.Fox
(2001).
Solution structure of the toluene 4-monooxygenase effector protein (T4moD).
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Biochemistry, 40,
3512-3524.
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PDB codes:
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H.Y.Kahng,
J.C.Malinverni,
M.M.Majko,
and
J.J.Kukor
(2001).
Genetic and functional analysis of the tbc operons for catabolism of alkyl- and chloroaromatic compounds in Burkholderia sp. strain JS150.
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Appl Environ Microbiol, 67,
4805-4816.
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M.Merkx,
D.A.Kopp,
M.H.Sazinsky,
J.L.Blazyk,
J.Müller,
and
S.J.Lippard
(2001).
Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins A list of abbreviations can be found in Section 7.
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Angew Chem Int Ed Engl, 40,
2782-2807.
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D.E.Coufal,
J.L.Blazyk,
D.A.Whittington,
W.W.Wu,
A.C.Rosenzweig,
and
S.J.Lippard
(2000).
Sequencing and analysis of the Mmethylococcus capsulatus (Bath) solublemethane monooxygenase genes.
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Eur J Biochem, 267,
2174-2185.
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Z.I.Finkelstein,
B.P.Baskunov,
M.G.Boersma,
J.Vervoort,
E.L.Golovlev,
W.J.van Berkel,
L.A.Golovleva,
and
I.M.Rietjens
(2000).
Identification of fluoropyrogallols as new intermediates in biotransformation of monofluorophenols in Rhodococcus opacus 1cp.
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Appl Environ Microbiol, 66,
2148-2153.
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E.Pessione,
S.Divari,
E.Griva,
M.Cavaletto,
G.L.Rossi,
G.Gilardi,
and
C.Giunta
(1999).
Phenol hydroxylase from Acinetobacter radioresistens is a multicomponent enzyme. Purification and characterization of the reductase moiety.
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Eur J Biochem, 265,
549-555.
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H.Brandstetter,
D.A.Whittington,
S.J.Lippard,
and
C.A.Frederick
(1999).
Mutational and structural analyses of the regulatory protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath).
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Chem Biol, 6,
441-449.
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K.J.Walters,
G.T.Gassner,
S.J.Lippard,
and
G.Wagner
(1999).
Structure of the soluble methane monooxygenase regulatory protein B.
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Proc Natl Acad Sci U S A, 96,
7877-7882.
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PDB code:
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N.Y.Zhou,
A.Jenkins,
C.K.Chan Kwo Chion,
and
D.J.Leak
(1999).
The alkene monooxygenase from Xanthobacter strain Py2 is closely related to aromatic monooxygenases and catalyzes aromatic monohydroxylation of benzene, toluene, and phenol.
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Appl Environ Microbiol, 65,
1589-1595.
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S.C.Gallagher,
A.J.Callaghan,
J.Zhao,
H.Dalton,
and
J.Trewhella
(1999).
Global conformational changes control the reactivity of methane monooxygenase.
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| |
Biochemistry, 38,
6752-6760.
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|
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S.L.Chang,
B.J.Wallar,
J.D.Lipscomb,
and
K.H.Mayo
(1999).
Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling.
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| |
Biochemistry, 38,
5799-5812.
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PDB code:
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|
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V.S.Bondar,
M.G.Boersma,
W.J.van Berkel,
Z.I.Finkelstein,
E.L.Golovlev,
B.P.Baskunov,
J.Vervoort,
L.A.Golovleva,
and
I.M.Rietjens
(1999).
Preferential oxidative dehalogenation upon conversion of 2-halophenols by Rhodococcus opacus 1G.
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| |
FEMS Microbiol Lett, 181,
73-82.
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|
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A.Ferrández,
B.Miñambres,
B.García,
E.R.Olivera,
J.M.Luengo,
J.L.García,
and
E.Díaz
(1998).
Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway.
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| |
J Biol Chem, 273,
25974-25986.
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G.Bertoni,
M.Martino,
E.Galli,
and
P.Barbieri
(1998).
Analysis of the gene cluster encoding toluene/o-xylene monooxygenase from Pseudomonas stutzeri OX1.
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Appl Environ Microbiol, 64,
3626-3632.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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