DB code: T00004

CATH domain 3.50.50.60 : FAD/NAD(P)-binding domain
4.10.450.10 : Glucose Oxidase; domain 2
3.30.560.10 : Glucose Oxidase; domain 3 Catalytic domain
E.C. 1.1.3.4
CSA 1gal
M-CSA 1gal
MACiE

CATH domain Related DB codes (homologues)
3.50.50.60 : FAD/NAD(P)-binding domain M00163 D00015 D00041 D00042 D00045 D00064 D00071 T00015 T00017 T00025 T00211 T00213 T00233 T00242

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P13006 Glucose oxidase
EC 1.1.3.4
Beta-D-glucose:oxygen 1-oxido-reductase
Glucose oxyhydrase
GOD
PF05199 (GMC_oxred_C)
PF00732 (GMC_oxred_N)
[Graphical View]
P81156 Glucose oxidase
EC 1.1.3.4
Beta-D-glucose:oxygen 1-oxido-reductase
Glucose oxyhydrase
GOD
PF05199 (GMC_oxred_C)
PF00732 (GMC_oxred_N)
[Graphical View]

KEGG enzyme name
glucose oxidase
glucose oxyhydrase
corylophyline
penatin
glucose aerodehydrogenase
microcid
beta-D-glucose oxidase
D-glucose oxidase
D-glucose-1-oxidase
beta-D-glucose:quinone oxidoreductase
glucose oxyhydrase
deoxin-1
GOD

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P81156 GOX_PENAG Beta-D-glucose + O(2) = D-glucono-1,5-lactone + H(2)O(2). Homodimer. Secreted. FAD.
P13006 GOX_ASPNG Beta-D-glucose + O(2) = D-glucono-1,5-lactone + H(2)O(2). Homodimer. Secreted. FAD.

KEGG Pathways
Map code Pathways E.C.
MAP00030 Pentose phosphate pathway

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00016 C00221 C00007 C00198 C00027
E.C.
Compound FAD beta-D-Glucose O2 D-Glucono-1,5-lactone H2O2
Type amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide carbohydrate others carbohydrate others
ChEBI 16238
15903
15379
26689
27140
16217
16240
PubChem 643975
64689
977
7027
22326046
784
1cf3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
1galA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
1gpeA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
1gpeB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1cf3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1galA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1gpeA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1gpeB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1cf3A03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1galA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1gpeA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1gpeB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P13006, P81156 & literature [16], [17], [18], [28], [29]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1cf3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 30;GLU 50;VAL 250;GLY 549(FAD binding)
1galA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 30;GLU 50;VAL 250;GLY 549(FAD binding)
1gpeA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 35;GLU 55;VAL 254;GLY 553(FAD binding)
1gpeB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 35;GLU 55;VAL 254;GLY 553(FAD binding)
1cf3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1galA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1gpeA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1gpeB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1cf3A03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 412;HIS 516;HIS 559
1galA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 412;HIS 516;HIS 559
1gpeA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 416;HIS 520;HIS 563
1gpeB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 416;HIS 520;HIS 563

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[11]
Fig.1, p.164-165
[15]
Fig.1, p.433-434, p.435-437, Fig.9
[16]
p.973-975
[17]
Scheme 1, p.8572-8573, p.8577-8578
[23]
p.3
[28]
p.81-82
[29]
Fig. 3, p.737-738, Fig.4, p.739-742, p.742-748

References
[1]
Resource
Comments
Medline ID
PubMed ID 7213598
Journal Biochemistry
Year 1981
Volume 20
Pages 617-21
Authors James TL, Edmondson DE, Husain M
Title Glucose oxidase contains a disubstituted phosphorus residue. Phosphorus-31 nuclear magnetic resonance studies of the flavin and nonflavin phosphate residues.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 6149727
Journal Arch Biochem Biophys
Year 1984
Volume 234
Pages 468-75
Authors Kido T, Soda K
Title Oxidation of anionic nitroalkanes by flavoenzymes, and participation of superoxide anion in the catalysis.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 2505251
Journal Proc Natl Acad Sci U S A
Year 1989
Volume 86
Pages 6493-7
Authors Johnson JL, London RE, Rajagopalan KV
Title Covalently bound phosphate residues in bovine milk xanthine oxidase and in glucose oxidase from Aspergillus niger: a reevaluation.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 2342102
Journal J Mol Biol
Year 1990
Volume 213
Pages 207-9
Authors Kalisz HM, Hecht HJ, Schomburg D, Schmid RD
Title Crystallization and preliminary X-ray diffraction studies of a deglycosylated glucose oxidase from Aspergillus niger.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 1772443
Journal Biochem Int
Year 1991
Volume 25
Pages 181-90
Authors Takegawa K, Kondo A, Iwamoto H, Fujiwara K, Hosokawa Y, Kato I, Hiromi K, Iwahara S
Title Novel oligomannose-type sugar chains derived from glucose oxidase of Aspergillus niger.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 2013289
Journal Eur J Biochem
Year 1991
Volume 196
Pages 663-72
Authors Sanner C, Macheroux P, Ruterjans H, Muller F, Bacher A
Title 15N- and 13C-NMR investigations of glucose oxidase from Aspergillus niger.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 1390684
Journal Biochemistry
Year 1992
Volume 31
Pages 8972-7
Authors Sierks MR, Bock K, Refn S, Svensson B
Title Active site similarities of glucose dehydrogenase, glucose oxidase, and glucoamylase probed by deoxygenated substrates.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 1542121
Journal J Mol Biol
Year 1992
Volume 223
Pages 811-4
Authors Cavener DR
Title GMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 1538394
Journal J Mol Biol
Year 1992
Volume 223
Pages 1167-9
Authors Hendle J, Hecht HJ, Kalisz HM, Schmid RD, Schomburg D
Title Crystallization and preliminary X-ray diffraction studies of a deglycosylated glucose oxidase from Penicillium amagasakiense.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 8357574
Journal Biosens Bioelectron
Year 1993
Volume 8
Pages 197-203
Authors Hecht HJ, Schomburg D, Kalisz H, Schmid RD
Title The 3D structure of glucose oxidase from Aspergillus niger. Implications for the use of GOD as a biosensor enzyme.
Related PDB
Related UniProtKB
[11]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID 93132782
PubMed ID 8421298
Journal J Mol Biol
Year 1993
Volume 229
Pages 153-72
Authors Hecht HJ, Kalisz HM, Hendle J, Schmid RD, Schomburg D
Title Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3 A resolution.
Related PDB 1gal
Related UniProtKB P13006
[12]
Resource
Comments
Medline ID
PubMed ID 9054567
Journal Biochemistry
Year 1997
Volume 36
Pages 2603-11
Authors Kohen A, Jonsson T, Klinman JP
Title Effects of protein glycosylation on catalysis: changes in hydrogen tunneling and enthalpy of activation in the glucose oxidase reaction.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 9463887
Journal Eur Biophys J
Year 1998
Volume 27
Pages 19-25
Authors Haouz A, Twist C, Zentz C, Tauc P, Alpert B
Title Dynamic and structural properties of glucose oxidase enzyme.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 9436625
Journal Free Radic Biol Med
Year 1998
Volume 24
Pages 155-60
Authors Metosh-Dickey CA, Mason RP, Winston GW
Title Single electron reduction of xenobiotic compounds by glucose oxidase from Aspergillus niger.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 9834905
Journal J Comput Aided Mol Des
Year 1998
Volume 12
Pages 425-40
Authors Meyer M, Wohlfahrt G, Knablein J, Schomburg D
Title Aspects of the mechanism of catalysis of glucose oxidase: a docking, molecular mechanics and quantum chemical study.
Related PDB
Related UniProtKB
[16]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Medline ID 99234348
PubMed ID 10216293
Journal Acta Crystallogr D Biol Crystallogr
Year 1999
Volume 55
Pages 969-77
Authors Wohlfahrt G, Witt S, Hendle J, Schomburg D, Kalisz HM, Hecht HJ
Title 1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes.
Related PDB 1gpe 1cf3
Related UniProtKB P13006 P81156
[17]
Resource
Comments
Medline ID
PubMed ID 10387105
Journal Biochemistry
Year 1999
Volume 38
Pages 8572-81
Authors Su Q, Klinman JP
Title Nature of oxygen activation in glucose oxidase from Aspergillus niger: the importance of electrostatic stabilization in superoxide formation.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 10749686
Journal Biochem J
Year 2000
Volume 347
Pages 553-9
Authors Witt S, Wohlfahrt G, Schomburg D, Hecht HJ, Kalisz HM
Title Conserved arginine-516 of Penicillium amagasakiense glucose oxidase is essential for the efficient binding of beta-D-glucose.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 10995249
Journal Biochemistry
Year 2000
Volume 39
Pages 11808-17
Authors Porter DJ, Voet JG, Bright HJ
Title Active site generation of a protonically unstable suicide substrate from a stable precursor: glucose oxidase and dibromonitromethane.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 11329261
Journal Biochemistry
Year 2001
Volume 40
Pages 1945-55
Authors Ahmad A, Akhtar MS, Bhakuni V
Title Monovalent cation-induced conformational change in glucose oxidase leading to stabilization of the enzyme.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 11602248
Journal FEBS Lett
Year 2001
Volume 506
Pages 216-20
Authors Haouz A, Glandieres JM, Alpert B
Title Involvement of protein dynamics in enzyme stability. The case of glucose oxidase.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 11720516
Journal Inorg Chem
Year 2001
Volume 40
Pages 6529-32
Authors Ryabov AD, Sukharev VS, Alexandrova L, Le Lagadec R, Pfeffer M
Title New synthesis and new bio-application of cyclometalated ruthenium(II) complexes for fast mediated electron transfer with peroxidase and glucose oxidase.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 11191216
Journal J Biol Inorg Chem
Year 2001
Volume 6
Pages 1-13
Authors Klinman JP
Title Life as aerobes: are there simple rules for activation of dioxygen by enzymes?
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 11592997
Journal Proc Natl Acad Sci U S A
Year 2001
Volume 98
Pages 11867-72
Authors Zhong D, Zewail AH
Title Femtosecond dynamics of flavoproteins: charge separation and recombination in riboflavine (vitamin B2)-binding protein and in glucose oxidase enzyme.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 12033948
Journal Biochemistry
Year 2002
Volume 41
Pages 7142-9
Authors Akhtar MS, Ahmad A, Bhakuni V
Title Divalent cation induced changes in structural properties of the dimeric enzyme glucose oxidase: dual effect of dimer stabilization and dissociation with loss of cooperative interactions in enzyme monomer.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 12716878
Journal J Biol Chem
Year 2003
Volume 278
Pages 24324-33
Authors Gouda MD, Singh SA, Rao AG, Thakur MS, Karanth NG
Title Thermal inactivation of glucose oxidase. Mechanism and stabilization using additives.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 15013780
Journal FEBS Lett
Year 2004
Volume 561
Pages 213-6
Authors Hosseinkhani S, Ranjbar B, Naderi-Manesh H, Nemat-Gorgani M
Title Chemical modification of glucose oxidase: possible formation of molten globule-like intermediate structure.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 15228088
Journal Mol Cell Biochem
Year 2004
Volume 260
Pages 69-83
Authors Wohlfahrt G, Trivic S, Zeremski J, Pericin D, Leskovac V
Title The chemical mechanism of action of glucose oxidase from Aspergillus niger.
Related PDB
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 15694834
Journal Int J Biochem Cell Biol
Year 2005
Volume 37
Pages 731-50
Authors Leskovac V, Trivic S, Wohlfahrt G, Kandrac J, Pericin D
Title Glucose oxidase from Aspergillus niger: the mechanism of action with molecular oxygen, quinones, and one-electron acceptors.
Related PDB
Related UniProtKB

Comments
According to the literature [29], this enzyme catalyzes two distinct reactions:
In reductive half-reaction, this enzyme catalyzes hydride transfer from glucose to FAD. In oxidative half-reaction, this enzyme catalyzes the production of peroxide from dioxygen. Moreover, this enzyme acts on quinone compounds in oxidative half-reaction.
(A) Hydride transfer from glucose to FAD, producing aldehyde and FADH2
(B) Hydride transfer from FADH2(reduced form) to O2, giving FAD and H2O2

Created Updated
2005-04-28 2009-02-26