T00004
type: Enzyme
cath: FAD/NAD(P)-binding domain
cath: Glucose Oxidase; domain 2
cath: Glucose Oxidase; domain 3
ec: https://purl.uniprot.org/enzyme/1.1.3.4
csa: 1gal
uniprot: P13006
uniprot: P81156
kegg enzyme: glucose oxidase
kegg enzyme: glucose oxyhydrase
kegg enzyme: corylophyline
kegg enzyme: penatin
kegg enzyme: glucose aerodehydrogenase
kegg enzyme: microcid
kegg enzyme: beta-D-glucose oxidase
kegg enzyme: D-glucose oxidase
kegg enzyme: D-glucose-1-oxidase
kegg enzyme: beta-D-glucose:quinone oxidoreductase
kegg enzyme: deoxin-1
kegg enzyme: GOD
kegg pathway: Pentose phosphate pathway
kegg cofactor: FAD
kegg substrate: beta-D-Glucose
kegg substrate: O2
kegg product: D-Glucono-1,5-lactone
kegg product: H2O2
pdb: 1cf3A01
pdb: 1galA01
pdb: 1gpeA01
pdb: 1gpeB01
pdb: 1cf3A02
pdb: 1galA02
pdb: 1gpeA02
pdb: 1gpeB02
pdb: 1cf3A03
pdb: 1galA03
pdb: 1gpeA03
pdb: 1gpeB03
pdb bound state: Unbound
  compound: beta-D-Glucose
  pdb: 1cf3A01
pdb bound state: Unbound
  compound: beta-D-Glucose
  pdb: 1galA01
pdb bound state: Unbound
  compound: beta-D-Glucose
  pdb: 1gpeA01
pdb bound state: Unbound
  compound: beta-D-Glucose
  pdb: 1gpeB01
pdb bound state: Unbound
  compound: beta-D-Glucose
  pdb: 1cf3A02
active site residues resources: Nature of oxygen activation in glucose oxidase from Aspergillus niger: the importance of electrostatic stabilization in superoxide formation.
active site residues resources: Conserved arginine-516 of Penicillium amagasakiense glucose oxidase is essential for the efficient binding of beta-D-glucose.
active site residues resources: Active site generation of a protonically unstable suicide substrate from a stable precursor: glucose oxidase and dibromonitromethane.
active site residues resources: Glucose oxidase from Aspergillus niger: the mechanism of action with molecular oxygen, quinones, and one-electron acceptors.
active site residues resources: http://ezcatdb.cbrc.jp/EzCatDB/reference/T00004#30
active site residues resources: P13006
active site residues resources: P81156
references: Glucose oxidase contains a disubstituted phosphorus residue. Phosphorus-31 nuclear magnetic resonance studies of the flavin and nonflavin phosphate residues.
references: Oxidation of anionic nitroalkanes by flavoenzymes, and participation of superoxide anion in the catalysis.
references: Covalently bound phosphate residues in bovine milk xanthine oxidase and in glucose oxidase from Aspergillus niger: a reevaluation.
references: Crystallization and preliminary X-ray diffraction studies of a deglycosylated glucose oxidase from Aspergillus niger.
references: Novel oligomannose-type sugar chains derived from glucose oxidase of Aspergillus niger.
references: 15N- and 13C-NMR investigations of glucose oxidase from Aspergillus niger.
references: Active site similarities of glucose dehydrogenase, glucose oxidase, and glucoamylase probed by deoxygenated substrates.
references: GMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities.
references: Crystallization and preliminary X-ray diffraction studies of a deglycosylated glucose oxidase from Penicillium amagasakiense.
references: The 3D structure of glucose oxidase from Aspergillus niger. Implications for the use of GOD as a biosensor enzyme.
references: Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3 A resolution.
references: Effects of protein glycosylation on catalysis: changes in hydrogen tunneling and enthalpy of activation in the glucose oxidase reaction.
references: Dynamic and structural properties of glucose oxidase enzyme.
references: Single electron reduction of xenobiotic compounds by glucose oxidase from Aspergillus niger.
references: Aspects of the mechanism of catalysis of glucose oxidase: a docking, molecular mechanics and quantum chemical study.
references: 1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes.
references: Nature of oxygen activation in glucose oxidase from Aspergillus niger: the importance of electrostatic stabilization in superoxide formation.
references: Conserved arginine-516 of Penicillium amagasakiense glucose oxidase is essential for the efficient binding of beta-D-glucose.
references: Active site generation of a protonically unstable suicide substrate from a stable precursor: glucose oxidase and dibromonitromethane.
references: Monovalent cation-induced conformational change in glucose oxidase leading to stabilization of the enzyme.
references: Involvement of protein dynamics in enzyme stability. The case of glucose oxidase.
references: New synthesis and new bio-application of cyclometalated ruthenium(II) complexes for fast mediated electron transfer with peroxidase and glucose oxidase.
references: Life as aerobes: are there simple rules for activation of dioxygen by enzymes?
references: Femtosecond dynamics of flavoproteins: charge separation and recombination in riboflavine (vitamin B2)-binding protein and in glucose oxidase enzyme.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/T00004#25
references: Thermal inactivation of glucose oxidase. Mechanism and stabilization using additives.
references: Chemical modification of glucose oxidase: possible formation of molten globule-like intermediate structure.
references: The chemical mechanism of action of glucose oxidase from Aspergillus niger.
references: Glucose oxidase from Aspergillus niger: the mechanism of action with molecular oxygen, quinones, and one-electron acceptors.
comment: 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

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

Glucose Oxidase; domain 2
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/4.10.450.10

Glucose Oxidase; domain 3
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.560.10
catalytic domain: index.html

Pentose phosphate pathway
type: KeggPathway
references: KEGG:MAP00030

FAD
type: KeggCofactor
references: KEGG:C00016
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: CHEBI:16238
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

beta-D-Glucose
type: KeggSubstrate
references: KEGG:C00221
compound type: carbohydrate
references: CHEBI:15903
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

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

D-Glucono-1,5-lactone
type: KeggProduct
references: KEGG:C00198
compound type: carbohydrate
references: CHEBI:16217
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

H2O2
type: KeggProduct
references: KEGG:C00027
compound type: others
references: CHEBI:16240
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1cf3A01
type: Pdb
references: 1cf3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cf3
cofactor binding residue: THR 30;GLU 50;VAL 250;GLY 549(FAD binding)

1galA01
type: Pdb
references: 1gal
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gal
cofactor binding residue: THR 30;GLU 50;VAL 250;GLY 549(FAD binding)

1gpeA01
type: Pdb
references: 1gpe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gpe
cofactor binding residue: THR 35;GLU 55;VAL 254;GLY 553(FAD binding)

1gpeB01
type: Pdb
references: 1gpe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gpe
cofactor binding residue: THR 35;GLU 55;VAL 254;GLY 553(FAD binding)

1cf3A03
type: Pdb
references: 1cf3
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cf3
catalytic residue: GLU 412;HIS 516;HIS 559

1galA03
type: Pdb
references: 1gal
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gal
catalytic residue: GLU 412;HIS 516;HIS 559

1gpeA03
type: Pdb
references: 1gpe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gpe
catalytic residue: GLU 416;HIS 520;HIS 563

1gpeB03
type: Pdb
references: 1gpe
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gpe
catalytic residue: GLU 416;HIS 520;HIS 563

Glucose oxidase contains a disubstituted phosphorus residue. Phosphorus-31 nuclear magnetic resonance studies of the flavin and nonflavin phosphate residues.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7213598
journal: Biochemistry
volume: 20
pages: 617-21
published year: 1981
authors:
  item: James TL
  item: Edmondson DE
  item: Husain M

Oxidation of anionic nitroalkanes by flavoenzymes, and participation of superoxide anion in the catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6149727
journal: Arch Biochem Biophys
volume: 234
pages: 468-75
published year: 1984
authors:
  item: Kido T
  item: Soda K

Covalently bound phosphate residues in bovine milk xanthine oxidase and in glucose oxidase from Aspergillus niger: a reevaluation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2505251
journal: Proc Natl Acad Sci U S A
volume: 86
pages: 6493-7
published year: 1989
authors:
  item: Johnson JL
  item: London RE
  item: Rajagopalan KV

Crystallization and preliminary X-ray diffraction studies of a deglycosylated glucose oxidase from Aspergillus niger.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2342102
journal: J Mol Biol
volume: 213
pages: 207-9
published year: 1990
authors:
  item: Kalisz HM
  item: Hecht HJ
  item: Schomburg D
  item: Schmid RD

Novel oligomannose-type sugar chains derived from glucose oxidase of Aspergillus niger.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1772443
journal: Biochem Int
volume: 25
pages: 181-90
published year: 1991
authors:
  item: Takegawa K
  item: Kondo A
  item: Iwamoto H
  item: Fujiwara K
  item: Hosokawa Y
  item: Kato I
  item: Hiromi K
  item: Iwahara S

15N- and 13C-NMR investigations of glucose oxidase from Aspergillus niger.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2013289
journal: Eur J Biochem
volume: 196
pages: 663-72
published year: 1991
authors:
  item: Sanner C
  item: Macheroux P
  item: Ruterjans H
  item: Muller F
  item: Bacher A

Active site similarities of glucose dehydrogenase, glucose oxidase, and glucoamylase probed by deoxygenated substrates.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1390684
journal: Biochemistry
volume: 31
pages: 8972-7
published year: 1992
authors:
  item: Sierks MR
  item: Bock K
  item: Refn S
  item: Svensson B

GMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1542121
journal: J Mol Biol
volume: 223
pages: 811-4
published year: 1992
authors:
  item: Cavener DR

Crystallization and preliminary X-ray diffraction studies of a deglycosylated glucose oxidase from Penicillium amagasakiense.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1538394
journal: J Mol Biol
volume: 223
pages: 1167-9
published year: 1992
authors:
  item: Hendle J
  item: Hecht HJ
  item: Kalisz HM
  item: Schmid RD
  item: Schomburg D

The 3D structure of glucose oxidase from Aspergillus niger. Implications for the use of GOD as a biosensor enzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8357574
journal: Biosens Bioelectron
volume: 8
pages: 197-203
published year: 1993
authors:
  item: Hecht HJ
  item: Schomburg D
  item: Kalisz H
  item: Schmid RD

Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3 A resolution.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
medline id: 93132782
references: http://www.ncbi.nlm.nih.gov/pubmed/8421298
journal: J Mol Biol
volume: 229
pages: 153-72
published year: 1993
authors:
  item: Hecht HJ
  item: Kalisz HM
  item: Hendle J
  item: Schmid RD
  item: Schomburg D
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P13006

Effects of protein glycosylation on catalysis: changes in hydrogen tunneling and enthalpy of activation in the glucose oxidase reaction.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9054567
journal: Biochemistry
volume: 36
pages: 2603-11
published year: 1997
authors:
  item: Kohen A
  item: Jonsson T
  item: Klinman JP

Dynamic and structural properties of glucose oxidase enzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9463887
journal: Eur Biophys J
volume: 27
pages: 19-25
published year: 1998
authors:
  item: Haouz A
  item: Twist C
  item: Zentz C
  item: Tauc P
  item: Alpert B

Single electron reduction of xenobiotic compounds by glucose oxidase from Aspergillus niger.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9436625
journal: Free Radic Biol Med
volume: 24
pages: 155-60
published year: 1998
authors:
  item: Metosh-Dickey CA
  item: Mason RP
  item: Winston GW

Aspects of the mechanism of catalysis of glucose oxidase: a docking, molecular mechanics and quantum chemical study.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9834905
journal: J Comput Aided Mol Des
volume: 12
pages: 425-40
published year: 1998
authors:
  item: Meyer M
  item: Wohlfahrt G
  item: Knablein J
  item: Schomburg D

1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
medline id: 99234348
references: http://www.ncbi.nlm.nih.gov/pubmed/10216293
journal: Acta Crystallogr D Biol Crystallogr
volume: 55
pages: 969-77
published year: 1999
authors:
  item: Wohlfahrt G
  item: Witt S
  item: Hendle J
  item: Schomburg D
  item: Kalisz HM
  item: Hecht HJ
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P13006
references: P81156

Nature of oxygen activation in glucose oxidase from Aspergillus niger: the importance of electrostatic stabilization in superoxide formation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10387105
journal: Biochemistry
volume: 38
pages: 8572-81
published year: 1999
authors:
  item: Su Q
  item: Klinman JP

Conserved arginine-516 of Penicillium amagasakiense glucose oxidase is essential for the efficient binding of beta-D-glucose.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10749686
journal: Biochem J
volume: 347
pages: 553-9
published year: 2000
authors:
  item: Witt S
  item: Wohlfahrt G
  item: Schomburg D
  item: Hecht HJ
  item: Kalisz HM

Active site generation of a protonically unstable suicide substrate from a stable precursor: glucose oxidase and dibromonitromethane.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10995249
journal: Biochemistry
volume: 39
pages: 11808-17
published year: 2000
authors:
  item: Porter DJ
  item: Voet JG
  item: Bright HJ

Monovalent cation-induced conformational change in glucose oxidase leading to stabilization of the enzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11329261
journal: Biochemistry
volume: 40
pages: 1945-55
published year: 2001
authors:
  item: Ahmad A
  item: Akhtar MS
  item: Bhakuni V

Involvement of protein dynamics in enzyme stability. The case of glucose oxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11602248
journal: FEBS Lett
volume: 506
pages: 216-20
published year: 2001
authors:
  item: Haouz A
  item: Glandieres JM
  item: Alpert B

New synthesis and new bio-application of cyclometalated ruthenium(II) complexes for fast mediated electron transfer with peroxidase and glucose oxidase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11720516
journal: Inorg Chem
volume: 40
pages: 6529-32
published year: 2001
authors:
  item: Ryabov AD
  item: Sukharev VS
  item: Alexandrova L
  item: Le Lagadec R
  item: Pfeffer M

Life as aerobes: are there simple rules for activation of dioxygen by enzymes?
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11191216
journal: J Biol Inorg Chem
volume: 6
pages: 1-13
published year: 2001
authors:
  item: Klinman JP

Femtosecond dynamics of flavoproteins: charge separation and recombination in riboflavine (vitamin B2)-binding protein and in glucose oxidase enzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11592997
journal: Proc Natl Acad Sci U S A
volume: 98
pages: 11867-72
published year: 2001
authors:
  item: Zhong D
  item: Zewail AH

http://ezcatdb.cbrc.jp/EzCatDB/reference/T00004#25
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12033948
journal: Biochemistry
volume: 41
pages: 7142-9
published year: 2002
authors:
  item: Akhtar MS
  item: Ahmad A
  item: 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.

Thermal inactivation of glucose oxidase. Mechanism and stabilization using additives.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12716878
journal: J Biol Chem
volume: 278
pages: 24324-33
published year: 2003
authors:
  item: Gouda MD
  item: Singh SA
  item: Rao AG
  item: Thakur MS
  item: Karanth NG

Chemical modification of glucose oxidase: possible formation of molten globule-like intermediate structure.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15013780
journal: FEBS Lett
volume: 561
pages: 213-6
published year: 2004
authors:
  item: Hosseinkhani S
  item: Ranjbar B
  item: Naderi-Manesh H
  item: Nemat-Gorgani M

The chemical mechanism of action of glucose oxidase from Aspergillus niger.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15228088
journal: Mol Cell Biochem
volume: 260
pages: 69-83
published year: 2004
authors:
  item: Wohlfahrt G
  item: Trivic S
  item: Zeremski J
  item: Pericin D
  item: Leskovac V

Glucose oxidase from Aspergillus niger: the mechanism of action with molecular oxygen, quinones, and one-electron acceptors.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15694834
journal: Int J Biochem Cell Biol
volume: 37
pages: 731-50
published year: 2005
authors:
  item: Leskovac V
  item: Trivic S
  item: Wohlfahrt G
  item: Kandrac J
  item: Pericin D

ReferenceForCatalyticMechanism
reference index: 11
reference section: Fig.1, p.164-165

ReferenceForCatalyticMechanism
reference index: 15
reference section: Fig.1, p.433-434, p.435-437, Fig.9

ReferenceForCatalyticMechanism
reference index: 16
reference section: p.973-975

ReferenceForCatalyticMechanism
reference index: 17
reference section: Scheme 1, p.8572-8573, p.8577-8578

ReferenceForCatalyticMechanism
reference index: 23
reference section: p.3

ReferenceForCatalyticMechanism
reference index: 28
reference section: p.81-82

ReferenceForCatalyticMechanism
reference index: 29
reference section: Fig. 3, p.737-738, Fig.4, p.739-742, p.742-748