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
Orthology
K00115  glucose 1-dehydrogenase (FAD, quinone)
K19813  glucose dehydrogenase
Genes
DME: Dmel_CG1152(Gld) Dmel_CG12398(CG12398)
DER: 6550630 6552663
DSI: Dsimw501_GD19489(Dsim_Gld) Dsimw501_GD22252(Dsim_GD22252)
DYA: Dyak_GE16083 Dyak_GE25798(Dyak_Gld)
DSR: 110187133 110188374
DPO: Dpse_GA11047(Dpse_Gld) Dpse_GA11607
DPE: 6594196 6602890
DMN: 108155759 108155806
DWI: 6641389 6647536
DGR: Dgri_GH11954 Dgri_GH19281
MDE: 101900331
VEM: 105561672
FCD: 110849883
YEN: YE1085
YEY: Y11_43071
YEW: CH47_501
YET: CH48_524
YAL: AT01_3557
YFR: AW19_277
YKR: CH54_1387
SMAF: D781_1913
DDQ: DDI_1993
EAY: EAM_1912
PAM: PANA_4103(adhB)
PLF: PANA5342_p10259(gdhA3)
PAJ: PAJ_p0187
PAQ: PAGR_p190
PSTW: DSJ_26130
LEZ: GLE_4831
LEM: LEN_4593
PCQ: PcP3B5_04810(fdhL)
PPF: Pput_4057
PPI: YSA_02456
PPX: T1E_3660
PFS: PFLU_3391
PFB: VO64_1302
PKC: PKB_0363
PSOS: POS17_0201
SBL: Sbal_1981
NHL: Nhal_3303
SLIM: SCL_1820
RSE: F504_790
RSY: RSUY_09890(fdhL)
RPI: Rpic_0719
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
BCEN: DM39_6100
BCEW: DM40_4560
BAM: Bamb_3978
BMU: Bmul_4094
BMK: DM80_5403
BMUL: NP80_4516
BCT: GEM_3905
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
BPH: Bphy_6262
HAR: HEAR2557
CFU: CFU_4430(sldL)
SUA: Saut_2066
SULC: CVO_01550
CFZ: CSG_19690
AHS: AHALO_2616(betA)
ARC: ABLL_1254
HOH: Hoch_1771
XAU: Xaut_0822
SNO: Snov_2174
BID: Bind_3801
MSC: BN69_1797
KVU: EIO_3193
KRO: BVG79_p1000117(tkrA)
MALG: MALG_03027
ZMN: Za10_0058
GOX: GOX2095
GOH: B932_3025
GXY: GLX_11570
GXL: H845_2331
KSC: CD178_01737(fdhL)
ASZ: ASN_3344
SALJ: SMD11_6007
SEN: SACE_4301
MAR: MAE_54660
AVA: Ava_4186
GBA: J421_2150
FLN: FLA_1894
PHE: Phep_1977
MUC: MuYL_2683
NDO: DDD_3127
HSL: OE_2509R
HHB: Hhub_2241
HHI: HAH_1116
HUT: Huta_1871
HTI: HTIA_1802
HMU: Hmuk_2378
HALL: LC1Hm_1738(betA)
HWA: HQ_3365A
HWC: Hqrw_3890
HME: HFX_1358(betA)
HLA: Hlac_0165
NAT: NJ7G_2196
SALI: L593_09535
 » 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
LinkDB All DBs

DBGET integrated database retrieval system