KEGG   ENZYME: 1.1.5.9Help
Entry
EC 1.1.5.9                  Enzyme                                 

Name
glucose 1-dehydrogenase (FAD, quinone);
glucose dehydrogenase (Aspergillus);
FAD-dependent glucose dehydrogenase;
D-glucose:(acceptor) 1-oxidoreductase;
glucose dehydrogenase (acceptor);
gdh (gene name)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With a quinone or similar compound as acceptor
BRITE hierarchy
Sysname
D-glucose:quinone 1-oxidoreductase
Reaction(IUBMB)
D-glucose + a quinone = D-glucono-1,5-lactone + a quinol [RN:R00305]
Reaction(KEGG)
Substrate
D-glucose [CPD:C00031];
quinone [CPD:C15602]
Product
D-glucono-1,5-lactone [CPD:C00198];
quinol [CPD:C15603]
Comment
A glycoprotein containing one mole of FAD per mole of enzyme. 2,6-Dichloroindophenol can act as acceptor. cf. EC 1.1.5.2, quinoprotein glucose dehydrogenase.
History
EC 1.1.5.9 created 1972 as 1.1.99.10, modified 1976, transferred 2013 to EC 1.1.5.9
Pathway
Pentose phosphate pathway
Metabolic pathways
Biosynthesis of secondary metabolites
Biosynthesis of antibiotics
Orthology
K00115  
glucose dehydrogenase (acceptor)
K19813  
glucose dehydrogenase
Genes
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
Dsimw501_GD15833(Dsim_GD15833) Dsimw501_GD22252(Dsim_GD22252)
DWI: 
DYA: 
Dyak_GE16083(dyak_GLEANR_17539) Dyak_GE16096(dyak_GLEANR_17550)
DGR: 
DMO: 
DVI: 
MDE: 
AGA: 
AAG: 
CQU: 
AME: 
552395(GMCOX2)
AEC: 
HST: 
CFO: 
NVI: 
TCA: 
API: 
PHU: 
YEN: 
YEP: 
YEY: 
YEW: 
YET: 
YEF: 
YEE: 
YAL: 
YFR: 
YKR: 
YAK: 
PAO: 
PDR: 
PKC: 
ACX: 
RSL: 
RSM: 
RSE: 
RPF: 
RMN: 
BMA: 
BMV: 
BML: 
BMN: 
BMAL: 
BMAE: 
BMAQ: 
BMAI: 
BMAF: 
BMAZ: 
BMAB: 
BPS: 
BPM: 
BPL: 
BPD: 
BPSE: 
BPSM: 
BPSU: 
BPSD: 
BPZ: 
BPQ: 
BPK: 
BPSH: 
BPSA: 
BPSO: 
BUT: 
BTE: 
BTQ: 
BTJ: 
BTZ: 
BTD: 
BTV: 
BTHE: 
BTHM: 
BTHA: 
BTHL: 
BOK: 
BOC: 
BVI: 
BVE: 
BUR: 
BCN: 
BCH: 
BCM: 
BCJ: 
BCEN: 
BCEW: 
BCEO: 
BAM: 
BAC: 
BMU: 
BMK: 
BMUL: 
BCT: 
BCED: 
BDL: 
BPYR: 
BCON: 
BUK: 
BUL: 
BUB: 
BUD: 
BFN: 
BCAI: 
CFU: 
CFU_4430(sldL)
CARE: 
CPRA: 
HOE: 
RLU: 
NGG: 
MSC: 
MALG: 
HAT: 
ZMM: 
ZMB: 
ZMI: 
ZMC: 
ZMR: 
ZMP: 
GOH: 
GOY: 
GXY: 
GXL: 
APW: 
APF: 
APU: 
APG: 
APQ: 
APX: 
APZ: 
APK: 
ASZ: 
 » show all
Taxonomy
Reference
1  [PMID:6034674]
  Authors
Bak TG.
  Title
Studies on glucose dehydrogenase of Aspergillus oryzae. II. Purification and physical and chemical properties.
  Journal
Biochim. Biophys. Acta. 139 (1967) 277-93.
Reference
2  [PMID:6413974]
  Authors
Cavener DR, MacIntyre RJ
  Title
Biphasic expression and function of glucose dehydrogenase in Drosophila melanogaster.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 80 (1983) 6286-8.
Reference
3  [PMID:12770264]
  Authors
Lovallo N, Cox-Foster DL
  Title
Alteration in FAD-glucose dehydrogenase activity and hemocyte behavior contribute to initial disruption of Manduca sexta immune response to Cotesia congregata parasitoids.
  Journal
J. Insect. Physiol. 45 (1999) 1037-1048.
Reference
4  [PMID:12573242]
  Authors
Inose K, Fujikawa M, Yamazaki T, Kojima K, Sode K
  Title
Cloning and expression of the gene encoding catalytic subunit of thermostable glucose dehydrogenase from Burkholderia cepacia in Escherichia coli.
  Journal
Biochim. Biophys. Acta. 1645 (2003) 133-8.
  Sequence
Reference
5  [PMID:21903757]
  Authors
Sygmund C, Klausberger M, Felice AK, Ludwig R
  Title
Reduction of quinones and phenoxy radicals by extracellular glucose dehydrogenase from Glomerella cingulata suggests a role in plant pathogenicity.
  Journal
Microbiology. 157 (2011) 3203-12.
Reference
6  [PMID:22151971]
  Authors
Sygmund C, Staudigl P, Klausberger M, Pinotsis N, Djinovic-Carugo K, Gorton L, Haltrich D, Ludwig R
  Title
Heterologous overexpression of Glomerella cingulata FAD-dependent glucose dehydrogenase in Escherichia coli and Pichia pastoris.
  Journal
Microb. Cell. Fact. 10 (2011) 106.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
37250-84-3

DBGET integrated database retrieval system