EzCatDB: T00005

DB codeT00005
CATH domainDomain 12.60.120.260
Domain 22.130.10.80Catalytic domain
Domain 32.60.40.10Catalytic domain
E.C.1.1.3.9
CSA1gog
MACiEM0322

CATH domainRelated DB codes (homologues)
2.60.120.260M00124,T00065,T00066
2.60.40.10M00131,T00257,M00113,M00127,M00132,M00323,M00325,M00327,M00329,M00330,M00331,M00332,T00307,D00166,D00500,M00112,M00193,T00063,T00065,T00067,T00245

Enzyme Name
Swiss-protKEGG

Q01745
Protein nameGalactose oxidasegalactose oxidase
D-galactose oxidase
beta-galactose oxidase
SynonymsGAO
GOase
GO
EC 1.1.3.9

KEGG pathways
MAP codePathways
MAP00052Galactose metabolism

Swiss-prot:Accession NumberQ01745
Entry nameGAOA_GIBZE
ActivityD-galactose + O(2) = D-galacto-hexodialdose + H(2)O(2).
SubunitMonomer.
Subcellular locationSecreted.
CofactorBinds 1 Cu(2+) ion per subunit.


CofactorsSubstratesProducts
KEGG-idC00070C00124C00007C03269C00027
CompoundCopperD-GalactoseO2D-Galacto-hexodialdoseH2O2
Typeheavy metalcarbohydrateotherscarbohydrateothers
1gofA01UnboundUnboundUnboundUnboundUnbound
1gogA01UnboundUnboundUnboundUnboundUnbound
1gohA01UnboundUnboundUnboundUnboundUnbound
1k3iA01UnboundUnboundUnboundUnboundUnbound
1t2xA01UnboundUnboundUnboundUnboundUnbound
1gofA02Bound:_CUUnboundUnboundAnalogue:ACY 703Unbound
1gogA02Bound:_CUUnboundUnboundUnboundUnbound
1gohA02UnboundUnboundUnboundUnboundUnbound
1k3iA02UnboundUnboundUnboundUnboundUnbound
1t2xA02Bound:_CUUnboundUnboundUnboundUnbound
1gofA03UnboundUnboundUnboundUnboundUnbound
1gogA03UnboundUnboundUnboundUnboundUnbound
1gohA03UnboundUnboundUnboundUnboundUnbound
1k3iA03UnboundUnboundUnboundUnboundUnbound
1t2xA03UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;Q01745 & literature [9], [14] & [32]
pdbCatalytic residuesCofactor-binding residuesModified residues
1gofA01


1gogA01


1gohA01


1k3iA01


1t2xA01


1gofA02CYS 228;TYR 272;TRP 290;TYR 495
TYR 272;TYR 495;HIS 496(Copper binding)

1gogA02CYS 228;TYR 272;TRP 290;TYR 495
TYR 272;TYR 495;HIS 496(Copper binding)

1gohA02CYS 228;TYR 272;TRP 290;TYR 495
TYR 272;TYR 495;HIS 496(Copper binding)

1k3iA02       ;TYR 272;TRP 290;TYR 495
TYR 272;TYR 495;HIS 496(Copper binding)
CSO 228
1t2xA02CYS 228;TYR 272;TRP 290;TYR 495
TYR 272;TYR 495;HIS 496(Copper binding)

1gofA03
HIS 581(Copper binding)

1gogA03
HIS 581(Copper binding)

1gohA03
HIS 581(Copper binding)

1k3iA03
HIS 581(Copper binding)

1t2xA03
HIS 581(Copper binding)


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[6]Fig.6
[9]p.88
[10]Fig.7, p.82-83
[12]Fig.9, p.770-771
[14]p.808-810
[15]Fig.1, p.510S
[18]Scheme 1, Scheme 4, Scheme 5
[19]Fig.8, Fig.9, p.8430-8435
[23]Fig.2, p.248-249
[26]Fig.4
[27]Scheme 1
[32]Fig.4, Fig.15, Fig.17, p.2358-2361

references
[1]
PubMed ID20059
JournalArch Biochem Biophys
Year1977
Volume182
Pages712-22
AuthorsKwiatkowski LD, Siconolfi L, Weiner RE, Giordano RS, Bereman RD, Ettinger MJ, Kosman DJ
TitleHistidine as an essential residue in the active site of the copper enzyme galactose oxidase.
[2]
PubMed ID902277
JournalCarbohydr Res
Year1977
Volume57
Pages273-80
AuthorsWhyte JN, Englar JR
TitleAn enzyme-P.M.R.-spectroscopic determination of the enantiomers of galactose.
[3]
PubMed ID6248103
JournalBiochemistry
Year1980
Volume19
Pages1304-8
AuthorsKosman DJ, Peisach J, Mims WB
TitlePulsed electron paramagnetic resonance studies of the copper(II) site in galactose oxidase.
[4]
PubMed ID7213759
JournalBiochim Biophys Acta
Year1981
Volume657
Pages495-506
AuthorsMarwedel BJ, Kurland RJ
TitleFluoride ion as an NMR relaxation probe of galactose oxidase-substrate binding.
[5]
PubMed ID6267193
JournalJ Inorg Biochem
Year1981
Volume14
Pages223-35
AuthorsWinkler ME, Bereman RD, Kurland RJ
TitleKinetic and magnetic resonance studies of substrate binding to galactose oxidase copper(II).
[6]
PubMed ID2834363
JournalJ Biol Chem
Year1988
Volume263
Pages6074-80
AuthorsWhittaker MM, Whittaker JW
TitleThe active site of galactose oxidase.
[7]
PubMed ID2542244
JournalJ Biol Chem
Year1989
Volume264
Pages7792-4
Authorsvan der Meer RA, Jongejan JA, Duine JA
TitlePyrroloquinoline quinone as cofactor in galactose oxidase (EC 1.1.3.9).
[8]
PubMed ID2161837
JournalJ Biol Chem
Year1990
Volume265
Pages9610-3
AuthorsWhittaker MM, Whittaker JW
TitleA tyrosine-derived free radical in apogalactose oxidase.
[9]
CommentsX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
Medline ID91163641
PubMed ID2002850
JournalNature
Year1991
Volume350
Pages87-90
AuthorsIto N, Phillips SE, Stevens C, Ogel ZB, McPherson MJ, Keen JN, Yadav KD, Knowles PF
TitleNovel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase.
Related PDB1gof,1gog,1goh
Related Swiss-protQ01745
[10]
PubMed ID1290941
JournalFaraday Discuss
Year1992
Volume-93
Pages75-84
AuthorsIto N, Phillips SE, Stevens C, Ogel ZB, McPherson MJ, Keen JN, Yadav KD, Knowles PF
TitleThree-dimensional structure of galactose oxidase: an enzyme with a built-in secondary cofactor.
[11]
PubMed ID8224464
JournalBiochem Soc Trans
Year1993
Volume21
Pages319S
AuthorsBaron AJ, Stevens C, Wilmot CM, Knowles PF, Phillips SE, McPherson MJ
TitlePreliminary studies of two active site mutants of galactose oxidase.
[12]
PubMed ID8386015
JournalBiophys J
Year1993
Volume64
Pages762-72
AuthorsWhittaker MM, Whittaker JW
TitleLigand interactions with galactose oxidase: mechanistic insights.
[13]
PubMed ID7929198
JournalJ Biol Chem
Year1994
Volume269
Pages25095-105
AuthorsBaron AJ, Stevens C, Wilmot C, Seneviratne KD, Blakeley V, Dooley DM, Phillips SE, Knowles PF, McPherson MJ
TitleStructure and mechanism of galactose oxidase. The free radical site.
[14]
PubMed ID8182749
JournalJ Mol Biol
Year1994
Volume238
Pages794-814
AuthorsIto N, Phillips SE, Yadav KD, Knowles PF
TitleCrystal structure of a free radical enzyme, galactose oxidase.
[15]
PubMed ID8654695
JournalBiochem Soc Trans
Year1995
Volume23
Pages510S
AuthorsReynolds MP, Baron AJ, Wilmot CM, Phillips SE, Knowles PF, McPherson MJ
TitleTyrosine 495 is a key residue in the active site of galactose oxidase.
[16]
PubMed ID8524154
JournalMethods Enzymol
Year1995
Volume258
Pages235-62
AuthorsIto N, Knowles PF, Phillips SE
TitleX-ray crystallographic studies of cofactors in galactose oxidase.
[17]
PubMed ID8524155
JournalMethods Enzymol
Year1995
Volume258
Pages262-77
AuthorsWhittaker JW
TitleSpectroscopic studies of galactose oxidase.
[18]
PubMed ID8916929
JournalBiochemistry
Year1996
Volume35
Pages14425-35
AuthorsWachter RM, Branchaud BP
TitleThiols as mechanistic probes for catalysis by the free radical enzyme galactose oxidase.
[19]
PubMed ID9622494
JournalBiochemistry
Year1998
Volume37
Pages8426-36
AuthorsWhittaker MM, Ballou DP, Whittaker JW
TitleKinetic isotope effects as probes of the mechanism of galactose oxidase.
[20]
PubMed ID9684896
JournalProtein Sci
Year1998
Volume7
Pages1626-31
AuthorsBaumgartner S, Hofmann K, Chiquet-Ehrismann R, Bucher P
TitleThe discoidin domain family revisited: new members from prokaryotes and a homology-based fold prediction.
[21]
PubMed ID9438841
JournalScience
Year1998
Volume279
Pages537-40
AuthorsWang Y, DuBois JL, Hedman B, Hodgson KO, Stack TD
TitleCatalytic galactose oxidase models: biomimetic Cu(II)-phenoxyl-radical reactivity.
[22]
PubMed ID10805536
JournalAnal Biochem
Year2000
Volume280
Pages173-7
AuthorsBasu SS, Dotson GD, Raetz CR
TitleA facile enzymatic synthesis of uridine diphospho-[14C]galacturonic acid.
[23]
PubMed ID10819469
JournalJ Biol Inorg Chem
Year2000
Volume5
Pages236-50
AuthorsRothlisberger U, Carloni P, Doclo K, Parrinello M
TitleA comparative study of galactose oxidase and active site analogs based on QM/MM Car-Parrinello simulations.
[24]
PubMed ID11948877
JournalChembiochem
Year2001
Volume2
Pages884-94
AuthorsBulter T, Schumacher T, Namdjou DJ, Gutierrez Gallego R, Clausen H, Elling L
TitleChemoenzymatic synthesis of biotinylated nucleotide sugars as substrates for glycosyltransferases.
[25]
PubMed ID11170534
JournalInorg Chem
Year2001
Volume40
Pages294-300
AuthorsWright C, Im SC, Twitchett MB, Saysell CG, Sokolowski A, Sykes AG
TitleThermodynamic, kinetic and pH studies on the reactions of NCS-, N3-, and CH3CO2- with Fusarium galactose oxidase.
[26]
PubMed ID11698678
JournalProc Natl Acad Sci U S A
Year2001
Volume98
Pages12932-7
AuthorsFirbank SJ, Rogers MS, Wilmot CM, Dooley DM, Halcrow MA, Knowles PF, McPherson MJ, Phillips SE
TitleCrystal structure of the precursor of galactose oxidase: an unusual self-processing enzyme.
Related PDB1k3i
[27]
PubMed ID12203454
JournalAngew Chem Int Ed Engl
Year2002
Volume41
Pages3047-50
AuthorsThomas F, Gellon G, Gautier-Luneau I, Saint-Aman E, Pierre JL
TitleA structural and functional model of galactose oxidase: control of the one-electron oxidized active form through two differentiated phenolic arms in a tripodal ligand.
[28]
PubMed ID12009437
JournalBioelectrochemistry
Year2002
Volume56
Pages23-5
AuthorsTkac J, Vostiar I, Gemeiner P, Sturdik E
TitleIndirect evidence of direct electron communication between the active site of galactose oxidase and a graphite electrode.
[29]
PubMed ID12058898
JournalJ Chromatogr A
Year2002
Volume954
Pages137-50
AuthorsMazitsos CF, Rigden DJ, Tsoungas PG, Clonis YD
TitleGalactosyl-biomimetic dye-ligands for the purification of Dactylium dendroides galactose oxidase.
[30]
PubMed ID12027633
JournalOrg Lett
Year2002
Volume4
Pages1863-6
AuthorsAndreana PR, Xie W, Cheng HN, Qiao L, Murphy DJ, Gu QM, Wang PG
TitleIn situ preparation of beta-D-1-O-hydroxylamino carbohydrate polymers mediated by galactose oxidase.
[31]
PubMed ID12027632
JournalOrg Lett
Year2002
Volume4
Pages1859-62
AuthorsChang D, Feiten HJ, Engesser KH, van Beilen JB, Witholt B, Li Z
TitlePractical syntheses of N-substituted 3-hydroxyazetidines and 4-hydroxypiperidines by hydroxylation with Sphingomonas sp. HXN-200.
[32]
PubMed ID12797833
JournalChem Rev
Year2003
Volume103
Pages2347-63
AuthorsWhittaker JW
TitleFree radical catalysis by galactose oxidase.
[33]
PubMed ID15047910
JournalProtein Eng Des Sel
Year2004
Volume17
Pages141-8
AuthorsWilkinson D, Akumanyi N, Hurtado-Guerrero R, Dawkes H, Knowles PF, Phillips SE, McPherson MJ
TitleStructural and kinetic studies of a series of mutants of galactose oxidase identified by directed evolution.
Related PDB1t2x

comments
This enzyme catalyze two distinct reactions:
(A) Reduction of alcohol substrate, to produce aldehyde. (Hydride transfer)
(B) Reduction of dioxygen (O2), to produce hydrogen peroxide (H2O2) (Hydride transfer)

createdupdated
2005-04-282009-02-26
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.