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, glucose 1-dehydrogenase (PQQ, quinone).
History
EC 1.1.5.9 created 1972 as EC 1.1.99.10, modified 1976, transferred 2013 to EC 1.1.5.9
Pathway
ec00030  Pentose phosphate pathway
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
ec01130  Biosynthesis of antibiotics
Orthology
K00115  glucose 1-dehydrogenase (FAD, quinone)
K19813  glucose dehydrogenase
Genes
DME: Dmel_CG1152(Gld) Dmel_CG12398(CG12398)
DER: 6550630 6552663
DSE: Dsec_GM10492(Dsec_Gld) Dsec_GM12018
DSI: Dsimw501_GD19489(Dsim_Gld) Dsimw501_GD22252(Dsim_GD22252)
DYA: Dyak_GE16083 Dyak_GE25798(Dyak_Gld)
DAN: Dana_GF17310 Dana_GF19424
DSR: 110187133 110188374
DPO: Dpse_GA11047(Dpse_Gld) Dpse_GA11607
DPE: 6594196 6602890
DMN: 108155759 108155806
DVI: Dvir_GJ10243(Dvir_Gld) Dvir_GJ16797
YEN: YE1085
YEY: Y11_43071
YEW: CH47_501
YET: CH48_524
YAL: AT01_3557
YFR: AW19_277
YKR: CH54_1387
SMAF: D781_1913
PCQ: PcP3B5_04810(fdhL)
PKC: PKB_0363
RSE: F504_790
RSY: RSUY_09890(fdhL)
BMA: BMAA1245
BMAL: DM55_4271
BMAE: DM78_3899
BMAQ: DM76_3223
BMAI: DM57_10785
BMAF: DM51_4906
BMAZ: BM44_4234
BMAB: BM45_3357
BPS: BPSS0976
BPSE: BDL_4271
BPSM: BBQ_5157
BPSU: BBN_4439
BPSD: BBX_6112
BPK: BBK_3457
BPSH: DR55_4356
BPSA: BBU_5052
BPSO: X996_4216
BUT: X994_6143
BTQ: BTQ_4702
BTJ: BTJ_5644
BTZ: BTL_4185
BTD: BTI_5797
BTV: BTHA_3774
BTHE: BTN_3508
BTHM: BTRA_4259
BTHA: DR62_3580
BTHL: BG87_4159
BOK: DM82_5143
BOC: BG90_5451
BVE: AK36_3808
BCN: Bcen_3815
BCJ: BCAM1735
BCEN: DM39_6100
BCEW: DM40_4560
BCEO: I35_5605
BAM: Bamb_3978
BMU: Bmul_4094
BMK: DM80_5403
BMUL: NP80_4516
BCT: GEM_3905
BCED: DM42_6214
BDL: AK34_3868
BCON: NL30_03470
BUB: BW23_5382
BLAT: WK25_25240
BTEI: WS51_06245
BSEM: WJ12_28605
BPSL: WS57_05330
BMEC: WJ16_27430
BSTG: WT74_27740
BUK: MYA_4130
BUL: BW21_5482
CFU: CFU_4430(sldL)
BID: Bind_3801
MSC: BN69_1797
MALG: MALG_03027
ZMN: Za10_0058
ZMM: Zmob_0060
ZMB: ZZ6_0063
ZMI: ZCP4_0058
GOH: B932_3025
GXY: GLX_11570
GXL: H845_2331
KSC: CD178_01737(fdhL)
ASZ: ASN_3344
GBA: J421_2150
 » 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 139:277-93 (1967)
DOI:10.1016/0005-2744(67)90032-0
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 80:6286-8 (1983)
DOI:10.1073/pnas.80.20.6286
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 45:1037-1048 (1999)
DOI:10.1016/S0022-1910(99)00086-4
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 1645:133-8 (2003)
DOI:10.1016/S1570-9639(02)00534-4
  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 157:3203-12 (2011)
DOI:10.1099/mic.0.051904-0
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 10:106 (2011)
DOI:10.1186/1475-2859-10-106
Other DBs
ExplorEnz - The Enzyme Database: 1.1.5.9
IUBMB Enzyme Nomenclature: 1.1.5.9
ExPASy - ENZYME nomenclature database: 1.1.5.9
BRENDA, the Enzyme Database: 1.1.5.9
CAS: 37250-84-3

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