EzCatDB: T00025
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DB codeT00025
CATH domainDomain 13.50.50.60 : FAD/NAD(P)-binding domainCatalytic domain
Domain 23.40.30.20 : Glutaredoxin
Domain 33.30.9.10 : D-Amino Acid Oxidase; Chain A, domain 2Catalytic domain
E.C.1.14.13.7
CSA1foh

CATH domainRelated DB codes (homologues)
3.30.9.10 : D-Amino Acid Oxidase; Chain A, domain 2D00037,D00041,D00064,D00494
3.50.50.60 : FAD/NAD(P)-binding domainM00163,D00015,D00041,D00042,D00045,D00064,D00071,T00004,T00015,T00017,T00211,T00213,T00233,T00242

Enzyme Name
UniProtKBKEGG

P15245
Protein namePhenol 2-monooxygenasephenol 2-monooxygenase
phenol hydroxylase
phenol o-hydroxylase
SynonymsEC 1.14.13.7
Phenol hydroxylase
PfamPF01494 (FAD_binding_3)
PF07976 (Phe_hydrox_dim)
[Graphical view]

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

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

Compound table: links to PDB-related databases & PoSSuM

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
ChEBI16238
15882
16474
27140
26689
15379
15378
18135
18009
15377
PubChem643975
996
20488062
5884
977
1038
289
5886
962
22247451
                
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 UniProtKBP15245
[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


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