D00064
type: Enzyme
active site residues resources: Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: the Tyr201Phe, Tyr385Phe, and Asn300Asp variants.
active site residues resources: 1cc4
active site residues resources: 1cc6
cath: FAD/NAD(P)-binding domain
cath: D-Amino Acid Oxidase; Chain A, domain 2
csa: 1dod
ec: https://purl.uniprot.org/enzyme/1.14.13.2
kegg cofactor: FAD
kegg enzyme: 4-hydroxybenzoate 3-monooxygenase
kegg pathway: Benzoate degradation via hydroxylation
kegg pathway: 2,4-Dichlorobenzoate degradation
kegg product: Protocatechuate
kegg product: NADP+
kegg product: H2O
kegg substrate: 4-Hydroxybenzoate
kegg substrate: NADPH
kegg substrate: O2
kegg substrate: H+
macie: M0131
pdb: 1bf3A01
pdb: 1bgjA01
pdb: 1bgnA01
pdb: 1bkwA01
pdb: 1cc4A01
pdb: 1cc6A01
pdb: 1cj2A01
pdb: 1cj3A01
pdb: 1cj4A01
pdb: 1d7lA01
pdb: 1dobA01
pdb: 1docA01
pdb: 1dodA01
pdb: 1doeA01
pdb: 1iusA01
pdb: 1iutA01
pdb: 1iuuA01
pdb: 1iuvA01
pdb: 1iuwA01
pdb: 1iuxA01
pdb: 1pbbA01
pdb: 1pbcA01
pdb: 1pbdA01
pdb: 1pbeA01
pdb: 1pbfA01
pdb: 1pdhA01
pdb: 1phhA01
pdb: 1pxaA01
pdb: 1pxbA01
pdb: 1pxcA01
pdb: 2phhA01
pdb: 1bf3A02
pdb: 1bgjA02
pdb: 1bgnA02
pdb: 1bkwA02
pdb: 1cc4A02
pdb: 1cc6A02
pdb: 1cj2A02
pdb: 1cj3A02
pdb: 1cj4A02
pdb: 1d7lA02
pdb: 1dobA02
pdb: 1docA02
pdb: 1dodA02
pdb: 1doeA02
pdb: 1iusA02
pdb: 1iutA02
pdb: 1iuuA02
pdb: 1iuvA02
pdb: 1iuwA02
pdb: 1iuxA02
pdb: 1pbbA02
pdb: 1pbcA02
pdb: 1pbdA02
pdb: 1pbeA02
pdb: 1pbfA02
pdb: 1pdhA02
pdb: 1phhA02
pdb: 1pxaA02
pdb: 1pxbA02

Analogue
compound: 4-Hydroxybenzoate
ligand het code: PAB
pdb: 1iusA02

Analogue
compound: 4-Hydroxybenzoate
ligand het code: PAB
pdb: 1iutA02

Analogue
compound: 4-Hydroxybenzoate
ligand het code: PAB
pdb: 1iuuA02

Analogue
compound: 4-Hydroxybenzoate
ligand het code: PAB
pdb: 1pbdA02

Analogue
compound: FAD
ligand het code: RFL
pdb: 1d7lA01

Analogue
compound: FAD
ligand het code: FAS
pdb: 1pdhA01

Analogue
compound: FAD
ligand het code: APR
pdb: 2phhA01

Analogue
compound: Protocatechuate
ligand het code: DOB
pdb: 1dodA02

Analogue
compound: Protocatechuate
ligand het code: DOB
pdb: 1doeA02

Analogue
compound: Protocatechuate
ligand het code: DOB
pdb: 1pbbA02

Analogue
compound: Protocatechuate
ligand het code: BHA
pdb: 1pbcA02

Analogue
compound: Protocatechuate
ligand het code: BHA
pdb: 1pbfA02

ReferenceForCatalyticMechanism
reference index: 3
reference section: p.72-73

ReferenceForCatalyticMechanism
reference index: 4
reference section: Fig.3, Fig.4

ReferenceForCatalyticMechanism
reference index: 5
reference section: Fig.3

ReferenceForCatalyticMechanism
reference index: 7
reference section: Fig.1, p.647

ReferenceForCatalyticMechanism
reference index: 10
reference section: Fig.1, Fig.2, Fig.6, Fig.7, Fig.8, p.3104-3106

ReferenceForCatalyticMechanism
reference index: 12
reference section: p.144-145

ReferenceForCatalyticMechanism
reference index: 13
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 14
reference section: Scheme 1

ReferenceForCatalyticMechanism
reference index: 16
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 18
reference section: Scheme 1, Scheme 2, Scheme 3, p.574-578

ReferenceForCatalyticMechanism
reference index: 24
reference section: Fig.1, Scheme 1, p.6294-6298

ReferenceForCatalyticMechanism
reference index: 25
reference section: Scheme 1, p.16641-16646

ReferenceForCatalyticMechanism
reference index: 30
reference section: Fig.1, p.170-172

ReferenceForCatalyticMechanism
reference index: 33
reference section: Scheme 2, Scheme 7

ReferenceForCatalyticMechanism
reference index: 36
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 37
reference section: Fig.1, p.22212-22215

ReferenceForCatalyticMechanism
reference index: 38
reference section: Fig.1, p.1573-1579

ReferenceForCatalyticMechanism
reference index: 39
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 40
reference section: Fig.1, p.305-309

D-Amino Acid Oxidase; Chain A, domain 2
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.30.9.10

FAD/NAD(P)-binding domain
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.50.50.60

H2O
type: KeggProduct
compound type: H2O
references: KEGG:C00001
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

H+
type: KeggSubstrate
compound type: others
references: KEGG:C00080
references: CHEBI:15378
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Benzoate degradation via hydroxylation
type: KeggPathway
references: KEGG:MAP00362

2,4-Dichlorobenzoate degradation
type: KeggPathway
references: KEGG:MAP00623

Crystallization and preliminary x-ray investigation of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.
type: BibliographicResource
authors:
  item: Drenth J
  item: Hol WG
  item: Wierenga RK
journal: J Biol Chem
pages: 5268-9
published year: 1975
volume: 250
references: http://www.ncbi.nlm.nih.gov/pubmed/807574

Analysis of the active site of the flavoprotein p-hydroxybenzoate hydroxylase and some ideas with respect to its reaction mechanism.
type: BibliographicResource
authors:
  item: Schreuder HA
  item: Hol WG
  item: Drenth J
journal: Biochemistry
pages: 3101-8
published year: 1990
volume: 29
references: http://www.ncbi.nlm.nih.gov/pubmed/2337581

Crystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3 A resolution.
type: BibliographicResource
authors:
  item: Schreuder HA
  item: van der Laan JM
  item: Swarte MB
  item: Kalk KH
  item: Hol WG
  item: Drenth J
journal: Proteins
medline id: 93028353
pages: 178-90
published year: 1992
volume: 14
references: http://www.ncbi.nlm.nih.gov/pubmed/1409567
references: P00438
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF REDUCED FORM

Role of Tyr201 and Tyr385 in substrate activation by p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.
type: BibliographicResource
authors:
  item: Eschrich K
  item: van der Bolt FJ
  item: de Kok A
  item: van Berkel WJ
journal: Eur J Biochem
pages: 137-46
published year: 1993
volume: 216
references: http://www.ncbi.nlm.nih.gov/pubmed/8365400

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00064#14
type: BibliographicResource
title: Crystal 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.
authors:
  item: Schreuder HA
  item: Mattevi A
  item: Obmolova G
  item: Kalk KH
  item: Hol WG
  item: van der Bolt FJ
  item: van Berkel WJ
journal: Biochemistry
pages: 10161-70
published year: 1994
volume: 33
references: http://www.ncbi.nlm.nih.gov/pubmed/7520279
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Crystal structure of p-hydroxybenzoate hydroxylase reconstituted with the modified FAD present in alcohol oxidase from methylotrophic yeasts: evidence for an arabinoflavin.
type: BibliographicResource
authors:
  item: van Berkel WJ
  item: Eppink MH
  item: Schreuder HA
journal: Protein Sci
pages: 2245-53
published year: 1994
volume: 3
references: http://www.ncbi.nlm.nih.gov/pubmed/7756982
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

The mobile flavin of 4-OH benzoate hydroxylase.
type: BibliographicResource
authors:
  item: Gatti DL
  item: Palfey BA
  item: Lah MS
  item: Entsch B
  item: Massey V
  item: Ballou DP
  item: Ludwig ML
journal: Science
medline id: 95025875
pages: 110-4
published year: 1994
volume: 266
references: http://www.ncbi.nlm.nih.gov/pubmed/7939628
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P20586
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)

Structure and function of mutant Arg44Lys of 4-hydroxybenzoate hydroxylase implications for NADPH binding.
type: BibliographicResource
authors:
  item: Eppink MH
  item: Schreuder HA
  item: Van Berkel WJ
journal: Eur J Biochem
medline id: 95354684
pages: 157-65
published year: 1995
volume: 231
references: http://www.ncbi.nlm.nih.gov/pubmed/7628466
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00438
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT LYS-44

pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis.
type: BibliographicResource
authors:
  item: Gatti DL
  item: Entsch B
  item: Ballou DP
  item: Ludwig ML
journal: Biochemistry
medline id: 96140232
pages: 567-78
published year: 1996
volume: 35
references: http://www.ncbi.nlm.nih.gov/pubmed/8555229
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P20586
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00064#19
type: BibliographicResource
title: 19F 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.
authors:
  item: van der Bolt FJ
  item: van den Heuvel RH
  item: Vervoort J
  item: van Berkel WJ
journal: Biochemistry
pages: 14192-201
published year: 1997
volume: 36
references: http://www.ncbi.nlm.nih.gov/pubmed/9369493

Electron microscopic studies on microcrystals of parahydroxybenzoate hydroxylase from Pseudomonas fluorescens.
type: BibliographicResource
authors:
  item: Marius A
  item: Schepman
  item: Schutter WG
  item: van Bruggen EF
journal: FEBS Lett
pages: 84-6
published year: 1976
volume: 65
references: http://www.ncbi.nlm.nih.gov/pubmed/819305

Identification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD/NAD(P)H binding.
type: BibliographicResource
authors:
  item: Eppink MH
  item: Schreuder HA
  item: Van Berkel WJ
journal: Protein Sci
pages: 2454-8
published year: 1997
volume: 6
references: http://www.ncbi.nlm.nih.gov/pubmed/9385648

The PHBH fold: not only flavoenzymes.
type: BibliographicResource
authors:
  item: Mattevi A
journal: Biophys Chem
pages: 217-22
published year: 1998
volume: 70
references: http://www.ncbi.nlm.nih.gov/pubmed/9546198

Lys42 and Ser42 variants of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens reveal that Arg42 is essential for NADPH binding.
type: BibliographicResource
authors:
  item: Eppink MH
  item: Schreuder HA
  item: van Berkel WJ
journal: Eur J Biochem
medline id: 98237589
pages: 194-201
published year: 1998
volume: 253
references: http://www.ncbi.nlm.nih.gov/pubmed/9578477
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00438
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT LYS-42 AND SER-42

Interdomain binding of NADPH in p-hydroxybenzoate hydroxylase as suggested by kinetic, crystallographic and modeling studies of histidine 162 and arginine 269 variants.
type: BibliographicResource
authors:
  item: Eppink MH
  item: Schreuder HA
  item: van Berkel WJ
journal: J Biol Chem
pages: 21031-9
published year: 1998
volume: 273
references: http://www.ncbi.nlm.nih.gov/pubmed/9694855
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Mechanistic insights into p-hydroxybenzoate hydroxylase from studies of the mutant Ser212Ala.
type: BibliographicResource
authors:
  item: Moran GR
  item: Entsch B
  item: Palfey BA
  item: Ballou DP
journal: Biochemistry
pages: 6292-9
published year: 1999
volume: 38
references: http://www.ncbi.nlm.nih.gov/pubmed/10320359

Structure-function correlations of the reaction of reduced nicotinamide analogues with p-hydroxybenzoate hydroxylase substituted with a series of 8-substituted flavins.
type: BibliographicResource
authors:
  item: Ortiz-Maldonado M
  item: Gatti D
  item: Ballou DP
  item: Massey V
journal: Biochemistry
pages: 16636-47
published year: 1999
volume: 38
references: http://www.ncbi.nlm.nih.gov/pubmed/10600126
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Substrate recognition by "password" in p-hydroxybenzoate hydroxylase.
type: BibliographicResource
authors:
  item: Palfey BA
  item: Moran GR
  item: Entsch B
  item: Ballou DP
  item: Massey V
journal: Biochemistry
pages: 1153-8
published year: 1999
volume: 38
references: http://www.ncbi.nlm.nih.gov/pubmed/9930974

Using Raman spectroscopy to monitor the solvent-exposed and "buried" forms of flavin in p-hydroxybenzoate hydroxylase.
type: BibliographicResource
authors:
  item: Zheng Y
  item: Dong J
  item: Palfey BA
  item: Carey PR
journal: Biochemistry
pages: 16727-32
published year: 1999
volume: 38
references: http://www.ncbi.nlm.nih.gov/pubmed/10606503

Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability.
type: BibliographicResource
authors:
  item: Eppink MH
  item: Bunthol C
  item: Schreuder HA
  item: van Berkel WJ
journal: FEBS Lett
medline id: 99148809
pages: 251-5
published year: 1999
volume: 443
references: http://www.ncbi.nlm.nih.gov/pubmed/10025942
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00438
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF VARIANTS

Switch of coenzyme specificity of p-hydroxybenzoate hydroxylase.
type: BibliographicResource
authors:
  item: Eppink MH
  item: Overkamp KM
  item: Schreuder HA
  item: Van Berkel WJ
journal: J Mol Biol
pages: 87-96
published year: 1999
volume: 292
references: http://www.ncbi.nlm.nih.gov/pubmed/10493859
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Crystal structure of p-hydroxybenzoate hydroxylase.
type: BibliographicResource
authors:
  item: Wierenga RK
  item: de Jong RJ
  item: Kalk KH
  item: Hol WG
  item: Drenth J
journal: J Mol Biol
medline id: 80029705
pages: 55-73
published year: 1979
volume: 131
references: http://www.ncbi.nlm.nih.gov/pubmed/40036
references: P00438
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)

Combined quantum mechanical and molecular mechanical reaction pathway calculation for aromatic hydroxylation by p-hydroxybenzoate-3-hydroxylase.
type: BibliographicResource
authors:
  item: Ridder L
  item: Mulholland AJ
  item: Rietjens IM
  item: Vervoort J
journal: J Mol Graph Model
pages: 163-75, 214
published year: 1999
volume: 17
references: http://www.ncbi.nlm.nih.gov/pubmed/10736773

Modelling flavin and substrate substituent effects on the activation barrier and rate of oxygen transfer by p-hydroxybenzoate hydroxylase.
type: BibliographicResource
authors:
  item: Ridder L
  item: Palfey BA
  item: Vervoort J
  item: Rietjens IM
journal: FEBS Lett
pages: 197-201
published year: 2000
volume: 478
references: http://www.ncbi.nlm.nih.gov/pubmed/10922496

Protein dynamics control proton transfers to the substrate on the His72Asn mutant of p-hydroxybenzoate hydroxylase.
type: BibliographicResource
authors:
  item: Frederick KK
  item: Ballou DP
  item: Palfey BA
journal: Biochemistry
pages: 3891-9
published year: 2001
volume: 40
references: http://www.ncbi.nlm.nih.gov/pubmed/11300768

A 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.
type: BibliographicResource
authors:
  item: Ortiz-Maldonado M
  item: Ballou DP
  item: Massey V
journal: Biochemistry
pages: 1091-101
published year: 2001
volume: 40
references: http://www.ncbi.nlm.nih.gov/pubmed/11170433

Comparing protein-ligand interactions in solution and single crystals by Raman spectroscopy.
type: BibliographicResource
authors:
  item: Altose MD
  item: Zheng Y
  item: Dong J
  item: Palfey BA
  item: Carey PR
journal: Proc Natl Acad Sci U S A
pages: 3006-11
published year: 2001
volume: 98
references: http://www.ncbi.nlm.nih.gov/pubmed/11248022

Protein and ligand dynamics in 4-hydroxybenzoate hydroxylase.
type: BibliographicResource
authors:
  item: Wang J
  item: Ortiz-Maldonado M
  item: Entsch B
  item: Massey V
  item: Ballou D
  item: Gatti DL
journal: Proc Natl Acad Sci U S A
pages: 608-13
published year: 2002
volume: 99
references: http://www.ncbi.nlm.nih.gov/pubmed/11805318

Conformational changes combined with charge-transfer interactions are essential for reduction in catalysis by p-hydroxybenzoate hydroxylase.
type: BibliographicResource
authors:
  item: Ortiz-Maldonado M
  item: Entsch B
  item: Ballou DP
journal: Biochemistry
pages: 11234-42
published year: 2003
volume: 42
references: http://www.ncbi.nlm.nih.gov/pubmed/14503873

Altered balance of half-reactions in p-hydroxybenzoate hydroxylase caused by substituting the 2'-carbon of FAD with fluorine.
type: BibliographicResource
authors:
  item: Palfey BA
  item: Murthy YV
  item: Massey V
journal: J Biol Chem
pages: 22210-6
published year: 2003
volume: 278
references: http://www.ncbi.nlm.nih.gov/pubmed/12684497

Increased positive electrostatic potential in p-hydroxybenzoate hydroxylase accelerates hydroxylation but slows turnover.
type: BibliographicResource
authors:
  item: Ortiz-Maldonado M
  item: Cole LJ
  item: Dumas SM
  item: Entsch B
  item: Ballou DP
journal: Biochemistry
pages: 1569-79
published year: 2004
volume: 43
references: http://www.ncbi.nlm.nih.gov/pubmed/14769033

Model studies on p-hydroxybenzoate hydroxylase. The catalytic role of Arg-214 and Tyr-201 in the hydroxylation step.
type: BibliographicResource
authors:
  item: Bach RD
  item: Dmitrenko O
journal: J Am Chem Soc
pages: 127-42
published year: 2004
volume: 126
references: http://www.ncbi.nlm.nih.gov/pubmed/14709077

Reaction mechanism of flavin-dependent hydroxylation. Evolution of a non-imitable enzyme.
type: BibliographicResource
authors:
  item: Visser CM
journal: Eur J Biochem
pages: 543-8
published year: 1983
volume: 135
references: http://www.ncbi.nlm.nih.gov/pubmed/6617648

Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase.
type: BibliographicResource
authors:
  item: Entsch B
  item: Cole LJ
  item: Ballou DP
journal: Arch Biochem Biophys
pages: 297-311
published year: 2005
volume: 433
references: http://www.ncbi.nlm.nih.gov/pubmed/15581585

Evolution of biocatalysis 4. Nicotinamide, flavin and dioxygen dependent hydroxylation. Origin of a non-imitable enzyme.
type: BibliographicResource
authors:
  item: Visser CM
journal: Orig Life
pages: 699-705
published year: 1984
volume: 14
references: http://www.ncbi.nlm.nih.gov/pubmed/6235473

Molecular modeling reveals the possible importance of a carbonyl oxygen binding pocket for the catalytic mechanism of p-hydroxybenzoate hydroxylase.
type: BibliographicResource
authors:
  item: Schreuder HA
  item: Hol WG
  item: Drenth J
journal: J Biol Chem
pages: 3131-6
published year: 1988
volume: 263
references: http://www.ncbi.nlm.nih.gov/pubmed/3343242

Crystal structure of p-hydroxybenzoate hydroxylase complexed with its reaction product 3,4-dihydroxybenzoate.
type: BibliographicResource
authors:
  item: Schreuder HA
  item: van der Laan JM
  item: Hol WG
  item: Drenth J
journal: J Mol Biol
medline id: 88172509
pages: 637-48
published year: 1988
volume: 199
references: http://www.ncbi.nlm.nih.gov/pubmed/3351945
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00438
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)

The coenzyme analogue adenosine 5-diphosphoribose displaces FAD in the active site of p-hydroxybenzoate hydroxylase. An x-ray crystallographic investigation.
type: BibliographicResource
authors:
  item: van der Laan JM
  item: Schreuder HA
  item: Swarte MB
  item: Wierenga RK
  item: Kalk KH
  item: Hol WG
  item: Drenth J
journal: Biochemistry
pages: 7199-205
published year: 1989
volume: 28
references: http://www.ncbi.nlm.nih.gov/pubmed/2819062
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 A resolution. Analysis of the enzyme-substrate and enzyme-product complexes.
type: BibliographicResource
authors:
  item: Schreuder HA
  item: Prick PA
  item: Wierenga RK
  item: Vriend G
  item: Wilson KS
  item: Hol WG
  item: Drenth J
journal: J Mol Biol
pages: 679-96
published year: 1989
volume: 208
references: http://www.ncbi.nlm.nih.gov/pubmed/2553983
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: the Tyr201Phe, Tyr385Phe, and Asn300Asp variants.
type: BibliographicResource
authors:
  item: Lah MS
  item: Palfey BA
  item: Schreuder HA
  item: Ludwig ML
journal: Biochemistry
medline id: 94146010
pages: 1555-64
published year: 1994
volume: 33
references: http://www.ncbi.nlm.nih.gov/pubmed/8312276
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P20586
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS

1bf3A01
type: Pdb
references: 1bf3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bf3
comment: mutant R42K, C116S

1bf3A02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1bf3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bf3
comment: invisible Y385

1bgjA01
type: Pdb
references: 1bgj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bgj
comment: mutant C116S, H162R

1bgjA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1bgj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bgj

1bgnA01
type: Pdb
references: 1bgn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bgn
comment: mutant C116S

1bgnA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1bgn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bgn
comment: mutant R269T

1bkwA01
type: Pdb
references: 1bkw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bkw
comment: mutant R44K, C116S

1bkwA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1bkw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1bkw

1cc4A01
type: Pdb
references: 1cc4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cc4
comment: mutant C116S, F161A

1cc4A02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1cc4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cc4

1cc6A01
type: Pdb
references: 1cc6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cc6
comment: mutant C116S, R166S

1cc6A02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1cc6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cc6

1cj2A01
type: Pdb
references: 1cj2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cj2
comment: mutant Q34R

1cj2A02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1cj2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cj2

1cj3A01
type: Pdb
references: 1cj3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cj3
comment: mutant Y38E

1cj3A02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1cj3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cj3

1cj4A01
type: Pdb
references: 1cj4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cj4
comment: mutant Q34T

1cj4A02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1cj4
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cj4

1d7lA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1d7l
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d7l

1dobA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1dob
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dob
comment: mutant Y222F

1docA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1doc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1doc

1iuvA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1iuv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iuv

1iuwA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1iuw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iuw

1iuxA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1iux
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iux

1pbbA01
type: Pdb
references: 1pbb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pbb
comment: mutant C116S

1pbcA01
type: Pdb
references: 1pbc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pbc
comment: mutant C116S

1pbdA01
type: Pdb
references: 1pbd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pbd
comment: mutant C116S

1pbeA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1pbe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pbe

1pbfA01
type: Pdb
references: 1pbf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pbf
comment: mutant C116S

1pdhA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1pdh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pdh

1phhA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1phh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1phh

1pxaA01
type: Pdb
references: 1pxa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pxa
comment: mutant N300D

1pxaA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1pxa
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pxa

1pxbA02
type: Pdb
catalytic residue: ;TYR 385
references: 1pxb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pxb
comment: mutant Y201F

1pxcA02
type: Pdb
catalytic residue: TYR 201;
references: 1pxc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pxc
comment: mutant Y385F

2phhA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 2phh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2phh

1dodA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1dod
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dod

1doeA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1doe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1doe

1iusA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1ius
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ius

1iutA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1iut
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iut

1iuuA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1iuu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iuu

1pbbA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1pbb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pbb

1pbcA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1pbc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pbc

1pbdA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1pbd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pbd

1pbfA02
type: Pdb
catalytic residue: TYR 201;TYR 385
references: 1pbf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pbf
comment: mutant Y222A

FAD
type: KeggCofactor
compound type: amide group
compound type: amine group
compound type: aromatic ring (only carbon atom)
compound type: aromatic ring (with nitrogen atoms)
compound type: carbohydrate
compound type: nucleotide
references: KEGG:C00016
references: CHEBI:16238
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

4-Hydroxybenzoate
type: KeggSubstrate
compound type: aromatic ring (only carbon atom)
compound type: carboxyl group
references: KEGG:C00156
references: CHEBI:30763
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Protocatechuate
type: KeggProduct
compound type: aromatic ring (only carbon atom)
compound type: carboxyl group
references: KEGG:C00230
references: CHEBI:36062
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADPH
type: KeggSubstrate
compound type: amide group
compound type: amine group
compound type: nucleotide
references: KEGG:C00005
references: CHEBI:16474
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADP+
type: KeggProduct
compound type: amide group
compound type: amine group
compound type: nucleotide
references: KEGG:C00006
references: CHEBI:18009
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

O2
type: KeggSubstrate
compound type: others
references: KEGG:C00007
references: CHEBI:15379
references: CHEBI:26689
references: CHEBI:27140
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

p-hydroxybenzoate hydrolyase
type: KeggEnzyme

p-hydroxybenzoate hydroxylase
type: KeggEnzyme

4-hydroxybenzoate 3-hydroxylase
type: KeggEnzyme

4-hydroxybenzoate monooxygenase
type: KeggEnzyme

4-hydroxybenzoic hydroxylase
type: KeggEnzyme

p-hydroxybenzoate-3-hydroxylase
type: KeggEnzyme

p-hydroxybenzoic acid hydrolase
type: KeggEnzyme

p-hydroxybenzoic acid hydroxylase
type: KeggEnzyme

p-hydroxybenzoic hydroxylase
type: KeggEnzyme