EzCatDB: T00025

DB codeT00025
CATH domainDomain 13.50.50.60Catalytic domain
Domain 23.40.30.20
Domain 33.30.9.10Catalytic domain
E.C.1.14.13.7
CSA1foh

CATH domainRelated DB codes (homologues)
3.30.9.10D00037,D00041,D00064,D00494
3.50.50.60M00163,D00015,D00041,D00042,D00045,D00064,D00071,T00004,T00015,T00017,T00211,T00213,T00233,T00242

Enzyme Name
Swiss-protKEGG

P15245
Protein namePhenol 2-monooxygenasephenol 2-monooxygenase
phenol hydroxylase
phenol o-hydroxylase
SynonymsEC 1.14.13.7
Phenol hydroxylase

KEGG pathways
MAP codePathways
MAP00361gamma-Hexachlorocyclohexane degradation
MAP00622Toluene and xylene degradation
MAP00626Naphthalene and anthracene degradation

Swiss-prot:Accession NumberP15245
Entry namePH2M_TRICU
ActivityPhenol + NADPH + O(2) = catechol + NADP(+) + H(2)O.
SubunitHomodimer.
Subcellular locationCytoplasm.
CofactorFAD.


CofactorsSubstratesProducts
KEGG-idC00016C00146C00005C00007C00080C00090C00006C00001
CompoundFADPhenolNADPHO2H+CatecholNADP+H2O
Typeamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotidearomatic ring (only carbon atom)amide group,amine group,nucleotideothersothersaromatic ring (only carbon atom)amide group,amine group,nucleotideH2O
1fohA01Bound:FADBound:IPHUnboundUnbound
UnboundUnbound
1fohB01Bound:FADBound:IPHUnboundUnbound
UnboundUnbound
1fohC01Bound:FADBound:IPHUnboundUnbound
UnboundUnbound
1fohD01Bound:FADBound:IPHUnboundUnbound
UnboundUnbound
1fohA02UnboundUnboundUnboundUnbound
UnboundUnbound
1fohB02UnboundUnboundUnboundUnbound
UnboundUnbound
1fohC02UnboundUnboundUnboundUnbound
UnboundUnbound
1fohD02UnboundUnboundUnboundUnbound
UnboundUnbound
1fohA03UnboundUnboundUnboundUnbound
UnboundUnbound
1fohB03UnboundUnboundUnboundUnbound
UnboundUnbound
1fohC03UnboundUnboundUnboundUnbound
UnboundUnbound
1fohD03UnboundUnboundUnboundUnbound
UnboundUnbound

Active-site residues
pdbCatalytic residues
1fohA01ASP 54
1fohB01ASP 54
1fohC01ASP 54
1fohD01ASP 54
1fohA02
1fohB02
1fohC02
1fohD02
1fohA03TYR 289
1fohB03TYR 289
1fohC03TYR 289
1fohD03TYR 289

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Fig.6
[6]Fig.8, p.613-614
[8]Scheme 1, Scheme 2
[11]Fig.10, Scheme 1

references
[1]
PubMed ID4146224
JournalEur J Biochem
Year1973
Volume35
Pages386-400
AuthorsNeujahr HY, Gaal A
TitlePhenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum.
[2]
PubMed ID2380181
JournalJ Biol Chem
Year1990
Volume265
Pages13687-94
AuthorsTaylor MG, Massey V
TitleDecay of the 4a-hydroxy-FAD intermediate of phenol hydroxylase.
[3]
PubMed ID8269923
JournalEur J Biochem
Year1993
Volume218
Pages345-53
AuthorsPeelen S, Rietjens IM, van Berkel WJ, van Workum WA, Vervoort J
Title19F-NMR study on the pH-dependent regioselectivity and rate of the ortho-hydroxylation of 3-fluorophenol by phenol hydroxylase from Trichosporon cutaneum. Implications for the reaction mechanism.
[4]
PubMed ID8145253
JournalJ Mol Biol
Year1994
Volume238
Pages128-30
AuthorsEnroth C, Huang W, Waters S, Neujahr H, Lindqvist Y, Schneider G
TitleCrystallization and preliminary X-ray analysis of phenol hydroxylase from Trichosporon cutaneum.
[5]
PubMed ID7851397
JournalEur J Biochem
Year1995
Volume227
Pages284-91
AuthorsPeelen S, Rietjens IM, Boersma MG, Vervoort J
TitleConversion of phenol derivatives to hydroxylated products by phenol hydroxylase from Trichosporon cutaneum. A comparison of regioselectivity and rate of conversion with calculated molecular orbital substrate characteristics.
[6]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)
Medline ID98298437
PubMed ID9634698
JournalStructure
Year1998
Volume6
Pages605-17
AuthorsEnroth C, Neujahr H, Schneider G, Lindqvist Y
TitleThe crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis.
Related PDB1foh
Related Swiss-protP15245
[7]
PubMed ID11082194
JournalEur J Biochem
Year2000
Volume267
Pages6832-40
AuthorsEppink MH, Cammaart E, Van Wassenaar D, Middelhoven WJ, van Berkel WJ
TitlePurification and properties of hydroquinone hydroxylase, a FAD-dependent monooxygenase involved in the catabolism of 4-hydroxybenzoate in Candida parapsilosis CBS604.
[8]
PubMed ID12427024
JournalBiochemistry
Year2002
Volume41
Pages13627-36
AuthorsXu D, Enroth C, Lindqvist Y, Ballou DP, Massey V
TitleStudies of the mechanism of phenol hydroxylase: effect of mutation of proline 364 to serine.
[9]
PubMed ID12653998
JournalEur J Biochem
Year2003
Volume270
Pages1434-40
AuthorsGriva E, Pessione E, Divari S, Valetti F, Cavaletto M, Rossi GL, Giunta C
TitlePhenol hydroxylase from Acinetobacter radioresistens S13. Isolation and characterization of the regulatory component.
[10]
PubMed ID12752444
JournalEur J Biochem
Year2003
Volume270
Pages2244-53
AuthorsDivari S, Valetti F, Caposio P, Pessione E, Cavaletto M, Griva E, Gribaudo G, Gilardi G, Giunta C
TitleThe oxygenase component of phenol hydroxylase from Acinetobacter radioresistens S13.
[11]
PubMed ID12968028
JournalJ Biol Chem
Year2003
Volume278
Pages47545-53
AuthorsKirchner U, Westphal AH, M?ller R, van Berkel WJ
TitlePhenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual role for FAD.
[12]
PubMed ID12925790
JournalActa Crystallogr D Biol Crystallogr
Year2003
Volume59
Pages1597-602
AuthorsEnroth C
TitleHigh-resolution structure of phenol hydroxylase and correction of sequence errors.
Related PDB1pn0

comments
According to the literature [6] and [8], this enzyme catalyzes the following reactions:
(A) Hydride transfer from NADH to FAD, producing NAD+ and FADH2:
(B) Oxygenation of phenol at FADH2 by O2, giving catechol, FAD and water (H2O):

createdupdated
2004-03-252009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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