EzCatDB: D00064

DB codeD00064
CATH domainDomain 13.50.50.60
Domain 23.30.9.10Catalytic domain
E.C.1.14.13.2
CSA1dod
MACiEM0131

CATH domainRelated DB codes (homologues)
3.30.9.10D00037,D00041,D00494,T00025
3.50.50.60M00163,D00015,D00041,D00042,D00045,D00071,T00004,T00015,T00017,T00025,T00211,T00213,T00233,T00242

Enzyme Name
Swiss-protKEGG

P20586P00438
Protein nameP-hydroxybenzoate hydroxylaseP-hydroxybenzoate hydroxylase4-hydroxybenzoate 3-monooxygenase
p-hydroxybenzoate hydrolyase
p-hydroxybenzoate hydroxylase
4-hydroxybenzoate 3-hydroxylase
4-hydroxybenzoate monooxygenase
4-hydroxybenzoic hydroxylase
p-hydroxybenzoate-3-hydroxylase
p-hydroxybenzoic acid hydrolase
p-hydroxybenzoic acid hydroxylase
p-hydroxybenzoic hydroxylase
SynonymsPHBH
EC 1.14.13.2
4-hydroxybenzoate 3-monooxygenase
EC 1.14.13.2
4-hydroxybenzoate 3-monooxygenase

KEGG pathways
MAP codePathways
MAP00362Benzoate degradation via hydroxylation
MAP006232,4-Dichlorobenzoate degradation

Swiss-prot:Accession NumberP20586P00438
Entry namePHHY_PSEAEPHHY_PSEFL
Activity4-hydroxybenzoate + NADPH + O(2) = protocatechuate + NADP(+) + H(2)O.4-hydroxybenzoate + NADPH + O(2) = protocatechuate + NADP(+) + H(2)O.
SubunitHomodimer.Homodimer.
Subcellular location

CofactorFAD.FAD.


CofactorsSubstratesProductsintermediates
KEGG-idC00016C00156C00005C00007C00080C00230C00006C00001

CompoundFAD4-HydroxybenzoateNADPHO2H+ProtocatechuateNADP+H2OFlavin 4a-hydroperoxide intermediateFlavin 4a-hydroxide intermediate
Typeamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotidearomatic ring (only carbon atom),carboxyl groupamide group,amine group,nucleotideothersothersaromatic ring (only carbon atom),carboxyl groupamide group,amine group,nucleotideH2O

1bf3A01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1bgjA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1bgnA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1bkwA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1cc4A01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1cc6A01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1cj2A01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1cj3A01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1cj4A01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1d7lA01Analogue:RFLUnboundUnboundUnbound
UnboundUnbound


1dobA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1docA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1dodA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1doeA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1iusA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1iutA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1iuuA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1iuvA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1iuwA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1iuxA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1pbbA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1pbcA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1pbdA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1pbeA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1pbfA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1pdhA01Analogue:FASUnboundUnboundUnbound
UnboundUnbound


1phhA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1pxaA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1pxbA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


1pxcA01Bound:FADUnboundUnboundUnbound
UnboundUnbound


2phhA01Analogue:APRUnboundUnboundUnbound
UnboundUnbound


1bf3A02UnboundBound:PHBUnboundUnbound
UnboundUnbound


1bgjA02UnboundBound:PHBUnboundUnbound
UnboundUnbound


1bgnA02UnboundBound:PHBUnboundUnbound
UnboundUnbound


1bkwA02UnboundBound:PHBUnboundUnbound
UnboundUnbound


1cc4A02UnboundBound:PHBUnboundUnbound
UnboundUnbound


1cc6A02UnboundBound:PHBUnboundUnbound
UnboundUnbound


1cj2A02UnboundBound:PHBUnboundUnbound
UnboundUnbound


1cj3A02UnboundBound:PHBUnboundUnbound
UnboundUnbound


1cj4A02UnboundBound:PHBUnboundUnbound
UnboundUnbound


1d7lA02UnboundBound:PHBUnboundUnbound
UnboundUnbound


1dobA02UnboundBound:PHBUnboundUnbound
UnboundUnbound


1docA02UnboundBound:PHBUnboundUnbound
UnboundUnbound


1dodA02UnboundUnboundUnboundUnbound
Analogue:DOBUnbound


1doeA02UnboundUnboundUnboundUnbound
Analogue:DOBUnbound


1iusA02UnboundAnalogue:PABUnboundUnbound
UnboundUnbound


1iutA02UnboundAnalogue:PABUnboundUnbound
UnboundUnbound


1iuuA02UnboundAnalogue:PABUnboundUnbound
UnboundUnbound


1iuvA02UnboundBound:PHBUnboundUnbound
UnboundUnbound


1iuwA02UnboundBound:PHBUnboundUnbound
UnboundUnbound


1iuxA02UnboundBound:PHBUnboundUnbound
UnboundUnbound


1pbbA02UnboundUnboundUnboundUnbound
Analogue:DOBUnbound


1pbcA02UnboundUnboundUnboundUnbound
Analogue:BHAUnbound


1pbdA02UnboundAnalogue:PABUnboundUnbound
UnboundUnbound


1pbeA02UnboundBound:PHBUnboundUnbound
UnboundUnbound


1pbfA02UnboundUnboundUnboundUnbound
Analogue:BHAUnbound


1pdhA02UnboundBound:PHBUnboundUnbound
UnboundUnbound


1phhA02UnboundUnboundUnboundUnbound
Bound:DHBUnbound


1pxaA02UnboundBound:PHBUnboundUnbound
UnboundUnbound


1pxbA02UnboundBound:PHBUnboundUnbound
UnboundUnbound


1pxcA02UnboundBound:PHBUnboundUnbound
UnboundUnbound


2phhA02UnboundBound:PHBUnboundUnbound
UnboundUnbound



Active-site residues
resource
PDB;1cc4, 1cc6 & literature [12]
pdbCatalytic residuescomment
1bf3A01               
mutant R42K, C116S
1bgjA01               
mutant C116S, H162R
1bgnA01               
mutant C116S
1bkwA01               
mutant R44K, C116S
1cc4A01               
mutant C116S, F161A
1cc6A01               
mutant C116S, R166S
1cj2A01               
mutant Q34R
1cj3A01               
mutant Y38E
1cj4A01               
mutant Q34T
1d7lA01               

1dobA01               

1docA01               

1dodA01               

1doeA01               

1iusA01               

1iutA01               

1iuuA01               

1iuvA01               

1iuwA01               

1iuxA01               

1pbbA01               
mutant C116S
1pbcA01               
mutant C116S
1pbdA01               
mutant C116S
1pbeA01               

1pbfA01               
mutant C116S
1pdhA01               

1phhA01               

1pxaA01               
mutant N300D
1pxbA01               

1pxcA01               

2phhA01               

1bf3A02TYR 201;TYR 385
invisible Y385
1bgjA02TYR 201;TYR 385

1bgnA02TYR 201;TYR 385
mutant R269T
1bkwA02TYR 201;TYR 385

1cc4A02TYR 201;TYR 385

1cc6A02TYR 201;TYR 385

1cj2A02TYR 201;TYR 385

1cj3A02TYR 201;TYR 385

1cj4A02TYR 201;TYR 385

1d7lA02TYR 201;TYR 385

1dobA02TYR 201;TYR 385
mutant Y222F
1docA02TYR 201;TYR 385

1dodA02TYR 201;TYR 385

1doeA02TYR 201;TYR 385

1iusA02TYR 201;TYR 385

1iutA02TYR 201;TYR 385

1iuuA02TYR 201;TYR 385

1iuvA02TYR 201;TYR 385

1iuwA02TYR 201;TYR 385

1iuxA02TYR 201;TYR 385

1pbbA02TYR 201;TYR 385

1pbcA02TYR 201;TYR 385

1pbdA02TYR 201;TYR 385

1pbeA02TYR 201;TYR 385

1pbfA02TYR 201;TYR 385
mutant Y222A
1pdhA02TYR 201;TYR 385

1phhA02TYR 201;TYR 385

1pxaA02TYR 201;TYR 385

1pxbA02       ;TYR 385
mutant Y201F
1pxcA02TYR 201;       
mutant Y385F
2phhA02TYR 201;TYR 385


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.72-73
[4]Fig.3, Fig.4
[5]Fig.3
[7]Fig.1, p.647
[10]Fig.1, Fig.2, Fig.6, Fig.7, Fig.8, p.3104-3106
[12]p.144-145
[13]Fig.1
[14]Scheme 1
[16]Fig.1
[18]Scheme 1, Scheme 2, Scheme 3, p.574-578
[24]Fig.1, Scheme 1, p.6294-6298
[25]Scheme 1, p.16641-16646
[30]Fig.1, p.170-172
[33]Scheme 2, Scheme 7
[36]Fig.1
[37]Fig.1, p.22212-22215
[38]Fig.1, p.1573-1579
[39]Fig.1
[40]Fig.1, p.305-309

references
[1]
PubMed ID807574
JournalJ Biol Chem
Year1975
Volume250
Pages5268-9
AuthorsDrenth J, Hol WG, Wierenga RK
TitleCrystallization and preliminary x-ray investigation of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.
[2]
PubMed ID819305
JournalFEBS Lett
Year1976
Volume65
Pages84-6
AuthorsMarius A, Schepman, Schutter WG, van Bruggen EF
TitleElectron microscopic studies on microcrystals of parahydroxybenzoate hydroxylase from Pseudomonas fluorescens.
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID80029705
PubMed ID40036
JournalJ Mol Biol
Year1979
Volume131
Pages55-73
AuthorsWierenga RK, de Jong RJ, Kalk KH, Hol WG, Drenth J
TitleCrystal structure of p-hydroxybenzoate hydroxylase.
Related Swiss-protP00438
[4]
PubMed ID6617648
JournalEur J Biochem
Year1983
Volume135
Pages543-8
AuthorsVisser CM
TitleReaction mechanism of flavin-dependent hydroxylation. Evolution of a non-imitable enzyme.
[5]
PubMed ID6235473
JournalOrig Life
Year1984
Volume14
Pages699-705
AuthorsVisser CM
TitleEvolution of biocatalysis 4. Nicotinamide, flavin and dioxygen dependent hydroxylation. Origin of a non-imitable enzyme.
[6]
PubMed ID3343242
JournalJ Biol Chem
Year1988
Volume263
Pages3131-6
AuthorsSchreuder HA, Hol WG, Drenth J
TitleMolecular modeling reveals the possible importance of a carbonyl oxygen binding pocket for the catalytic mechanism of p-hydroxybenzoate hydroxylase.
[7]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)
Medline ID88172509
PubMed ID3351945
JournalJ Mol Biol
Year1988
Volume199
Pages637-48
AuthorsSchreuder HA, van der Laan JM, Hol WG, Drenth J
TitleCrystal structure of p-hydroxybenzoate hydroxylase complexed with its reaction product 3,4-dihydroxybenzoate.
Related PDB1phh
Related Swiss-protP00438
[8]
CommentsX-ray crystallography
PubMed ID2819062
JournalBiochemistry
Year1989
Volume28
Pages7199-205
Authorsvan der Laan JM, Schreuder HA, Swarte MB, Wierenga RK, Kalk KH, Hol WG, Drenth J
TitleThe coenzyme analogue adenosine 5-diphosphoribose displaces FAD in the active site of p-hydroxybenzoate hydroxylase. An x-ray crystallographic investigation.
Related PDB2phh
[9]
CommentsX-ray crystallography
PubMed ID2553983
JournalJ Mol Biol
Year1989
Volume208
Pages679-96
AuthorsSchreuder HA, Prick PA, Wierenga RK, Vriend G, Wilson KS, Hol WG, Drenth J
TitleCrystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 A resolution. Analysis of the enzyme-substrate and enzyme-product complexes.
Related PDB1pbe
[10]
PubMed ID2337581
JournalBiochemistry
Year1990
Volume29
Pages3101-8
AuthorsSchreuder HA, Hol WG, Drenth J
TitleAnalysis of the active site of the flavoprotein p-hydroxybenzoate hydroxylase and some ideas with respect to its reaction mechanism.
[11]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF REDUCED FORM
Medline ID93028353
PubMed ID1409567
JournalProteins
Year1992
Volume14
Pages178-90
AuthorsSchreuder HA, van der Laan JM, Swarte MB, Kalk KH, Hol WG, Drenth J
TitleCrystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3 A resolution.
Related Swiss-protP00438
[12]
PubMed ID8365400
JournalEur J Biochem
Year1993
Volume216
Pages137-46
AuthorsEschrich K, van der Bolt FJ, de Kok A, van Berkel WJ
TitleRole of Tyr201 and Tyr385 in substrate activation by p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.
[14]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS
Medline ID94146010
PubMed ID8312276
JournalBiochemistry
Year1994
Volume33
Pages1555-64
AuthorsLah MS, Palfey BA, Schreuder HA, Ludwig ML
TitleCrystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: the Tyr201Phe, Tyr385Phe, and Asn300Asp variants.
Related PDB1pxa,1pxb,1pxc
Related Swiss-protP20586
[13]
CommentsX-ray crystallography
PubMed ID7520279
JournalBiochemistry
Year1994
Volume33
Pages10161-70
AuthorsSchreuder HA, Mattevi A, Obmolova G, Kalk KH, Hol WG, van der Bolt FJ, van Berkel WJ
TitleCrystal structures of wild-type p-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate,2,4-dihydroxybenzoate, and 2-hydroxy-4-aminobenzoate and of the Tyr222Ala mutant complexed with 2-hydroxy-4-aminobenzoate. Evidence for a proton channel and a new binding mode of the flavin ring.
Related PDB1pbb,1pbc,1pbd,1pbf
[15]
CommentsX-ray crystallography
PubMed ID7756982
JournalProtein Sci
Year1994
Volume3
Pages2245-53
Authorsvan Berkel WJ, Eppink MH, Schreuder HA
TitleCrystal structure of p-hydroxybenzoate hydroxylase reconstituted with the modified FAD present in alcohol oxidase from methylotrophic yeasts: evidence for an arabinoflavin.
Related PDB1pdh
[16]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID95025875
PubMed ID7939628
JournalScience
Year1994
Volume266
Pages110-4
AuthorsGatti DL, Palfey BA, Lah MS, Entsch B, Massey V, Ballou DP, Ludwig ML
TitleThe mobile flavin of 4-OH benzoate hydroxylase.
Related PDB1dob,1doc,1dod,1doe
Related Swiss-protP20586
[17]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT LYS-44
Medline ID95354684
PubMed ID7628466
JournalEur J Biochem
Year1995
Volume231
Pages157-65
AuthorsEppink MH, Schreuder HA, Van Berkel WJ
TitleStructure and function of mutant Arg44Lys of 4-hydroxybenzoate hydroxylase implications for NADPH binding.
Related PDB1bkw
Related Swiss-protP00438
[18]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID96140232
PubMed ID8555229
JournalBiochemistry
Year1996
Volume35
Pages567-78
AuthorsGatti DL, Entsch B, Ballou DP, Ludwig ML
TitlepH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis.
Related PDB1ius,1iut,1iuu,1iuv,1iuw,1iux
Related Swiss-protP20586
[19]
PubMed ID9369493
JournalBiochemistry
Year1997
Volume36
Pages14192-201
Authorsvan der Bolt FJ, van den Heuvel RH, Vervoort J, van Berkel WJ
Title19F NMR study on the regiospecificity of hydroxylation of tetrafluoro-4-hydroxybenzoate by wild-type and Y385F p-hydroxybenzoate hydroxylase: evidence for a consecutive oxygenolytic dehalogenation mechanism.
[20]
PubMed ID9385648
JournalProtein Sci
Year1997
Volume6
Pages2454-8
AuthorsEppink MH, Schreuder HA, Van Berkel WJ
TitleIdentification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD/NAD(P)H binding.
[21]
PubMed ID9546198
JournalBiophys Chem
Year1998
Volume70
Pages217-22
AuthorsMattevi A
TitleThe PHBH fold: not only flavoenzymes.
[22]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT LYS-42 AND SER-42
Medline ID98237589
PubMed ID9578477
JournalEur J Biochem
Year1998
Volume253
Pages194-201
AuthorsEppink MH, Schreuder HA, van Berkel WJ
TitleLys42 and Ser42 variants of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens reveal that Arg42 is essential for NADPH binding.
Related PDB1bf3
Related Swiss-protP00438
[23]
CommentsX-ray crystallography
PubMed ID9694855
JournalJ Biol Chem
Year1998
Volume273
Pages21031-9
AuthorsEppink MH, Schreuder HA, van Berkel WJ
TitleInterdomain binding of NADPH in p-hydroxybenzoate hydroxylase as suggested by kinetic, crystallographic and modeling studies of histidine 162 and arginine 269 variants.
Related PDB1bgj,1bgn
[24]
PubMed ID10320359
JournalBiochemistry
Year1999
Volume38
Pages6292-9
AuthorsMoran GR, Entsch B, Palfey BA, Ballou DP
TitleMechanistic insights into p-hydroxybenzoate hydroxylase from studies of the mutant Ser212Ala.
[25]
CommentsX-ray crystallography
PubMed ID10600126
JournalBiochemistry
Year1999
Volume38
Pages16636-47
AuthorsOrtiz-Maldonado M, Gatti D, Ballou DP, Massey V
TitleStructure-function correlations of the reaction of reduced nicotinamide analogues with p-hydroxybenzoate hydroxylase substituted with a series of 8-substituted flavins.
Related PDB1d7l
[26]
PubMed ID9930974
JournalBiochemistry
Year1999
Volume38
Pages1153-8
AuthorsPalfey BA, Moran GR, Entsch B, Ballou DP, Massey V
TitleSubstrate recognition by "password" in p-hydroxybenzoate hydroxylase.
[27]
PubMed ID10606503
JournalBiochemistry
Year1999
Volume38
Pages16727-32
AuthorsZheng Y, Dong J, Palfey BA, Carey PR
TitleUsing Raman spectroscopy to monitor the solvent-exposed and "buried" forms of flavin in p-hydroxybenzoate hydroxylase.
[28]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF VARIANTS
Medline ID99148809
PubMed ID10025942
JournalFEBS Lett
Year1999
Volume443
Pages251-5
AuthorsEppink MH, Bunthol C, Schreuder HA, van Berkel WJ
TitlePhe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability.
Related PDB1cc4,1cc6
Related Swiss-protP00438
[29]
CommentsX-ray crystallography
PubMed ID10493859
JournalJ Mol Biol
Year1999
Volume292
Pages87-96
AuthorsEppink MH, Overkamp KM, Schreuder HA, Van Berkel WJ
TitleSwitch of coenzyme specificity of p-hydroxybenzoate hydroxylase.
Related PDB1cj2,1cj3,1cj4
[30]
PubMed ID10736773
JournalJ Mol Graph Model
Year1999
Volume17
Pages163-75, 214
AuthorsRidder L, Mulholland AJ, Rietjens IM, Vervoort J
TitleCombined quantum mechanical and molecular mechanical reaction pathway calculation for aromatic hydroxylation by p-hydroxybenzoate-3-hydroxylase.
[31]
PubMed ID10922496
JournalFEBS Lett
Year2000
Volume478
Pages197-201
AuthorsRidder L, Palfey BA, Vervoort J, Rietjens IM
TitleModelling flavin and substrate substituent effects on the activation barrier and rate of oxygen transfer by p-hydroxybenzoate hydroxylase.
[32]
PubMed ID11300768
JournalBiochemistry
Year2001
Volume40
Pages3891-9
AuthorsFrederick KK, Ballou DP, Palfey BA
TitleProtein dynamics control proton transfers to the substrate on the His72Asn mutant of p-hydroxybenzoate hydroxylase.
[33]
PubMed ID11170433
JournalBiochemistry
Year2001
Volume40
Pages1091-101
AuthorsOrtiz-Maldonado M, Ballou DP, Massey V
TitleA rate-limiting conformational change of the flavin in p-hydroxybenzoate hydroxylase is necessary for ligand exchange and catalysis: studies with 8-mercapto- and 8-hydroxy-flavins.
[34]
PubMed ID11248022
JournalProc Natl Acad Sci U S A
Year2001
Volume98
Pages3006-11
AuthorsAltose MD, Zheng Y, Dong J, Palfey BA, Carey PR
TitleComparing protein-ligand interactions in solution and single crystals by Raman spectroscopy.
[35]
PubMed ID11805318
JournalProc Natl Acad Sci U S A
Year2002
Volume99
Pages608-13
AuthorsWang J, Ortiz-Maldonado M, Entsch B, Massey V, Ballou D, Gatti DL
TitleProtein and ligand dynamics in 4-hydroxybenzoate hydroxylase.
[36]
PubMed ID14503873
JournalBiochemistry
Year2003
Volume42
Pages11234-42
AuthorsOrtiz-Maldonado M, Entsch B, Ballou DP
TitleConformational changes combined with charge-transfer interactions are essential for reduction in catalysis by p-hydroxybenzoate hydroxylase.
[37]
PubMed ID12684497
JournalJ Biol Chem
Year2003
Volume278
Pages22210-6
AuthorsPalfey BA, Murthy YV, Massey V
TitleAltered balance of half-reactions in p-hydroxybenzoate hydroxylase caused by substituting the 2'-carbon of FAD with fluorine.
[38]
PubMed ID14769033
JournalBiochemistry
Year2004
Volume43
Pages1569-79
AuthorsOrtiz-Maldonado M, Cole LJ, Dumas SM, Entsch B, Ballou DP
TitleIncreased positive electrostatic potential in p-hydroxybenzoate hydroxylase accelerates hydroxylation but slows turnover.
[39]
PubMed ID14709077
JournalJ Am Chem Soc
Year2004
Volume126
Pages127-42
AuthorsBach RD, Dmitrenko O
TitleModel studies on p-hydroxybenzoate hydroxylase. The catalytic role of Arg-214 and Tyr-201 in the hydroxylation step.
[40]
PubMed ID15581585
JournalArch Biochem Biophys
Year2005
Volume433
Pages297-311
AuthorsEntsch B, Cole LJ, Ballou DP
TitleProtein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase.

comments
According to the literature [10], [13], [14] & [40], this enzyme catalyzes the following reactions:
(A) Hydride transfer from NADPH to FAD, forming FADH2 (Reduction of FAD by NADPH) (Reductive half-reaction):
(B) Oxygenation of hydroxybenzoate by O2 at FADH2 (Oxidative half-reaction):
(B1) Oxygenation to form a flavin 4a-hydroperoxide intermediate.
(B2) Additive double-bond deformation; Addition of hydroxyl group to substrate, 4-hydroxybenzoate, by flavin 4a-hydroperoxide intermediate (Hydroxylation of substrate), forming 3,4-dihydroxybenzoate and a flavin 4a-hydroxide intermediate.
(B3) Eliminative double-bond formation; Elimination of H2O from flavin 4a-hydroxide intermediate, giving FAD.

createdupdated
2004-03-242009-02-26


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)

© Computational Biology Research Center, AIST, 2004 All Rights Reserved.