KEGG   ENZYME: 1.1.5.2Help
Entry
EC 1.1.5.2                  Enzyme                                 

Name
glucose 1-dehydrogenase (PQQ, quinone);
quinoprotein glucose dehydrogenase;
membrane-bound glucose dehydrogenase;
mGDH;
glucose dehydrogenase (PQQ-dependent);
glucose dehydrogenase (pyrroloquinoline-quinone);
quinoprotein D-glucose dehydrogenase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With a quinone or similar compound as acceptor
BRITE hierarchy
Sysname
D-glucose:ubiquinone oxidoreductase
Reaction(IUBMB)
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol [RN:R06620]
Reaction(KEGG)
Substrate
D-glucose [CPD:C00031];
ubiquinone [CPD:C00399]
Product
D-glucono-1,5-lactone [CPD:C00198];
ubiquinol [CPD:C00390]
Comment
Integral membrane protein containing PQQ as prosthetic group. It also contains bound ubiquinone and Mg2+ or Ca2+. Electron acceptor is membrane ubiquinone but usually assayed with phenazine methosulfate. Like in all other quinoprotein alcohol dehydrogenases the catalytic domain has an 8-bladed propeller structure. It occurs in a wide range of bacteria. Catalyses a direct oxidation of the pyranose form of D-glucose to the lactone and thence to D-gluconate in the periplasm. Oxidizes other monosaccharides including the pyranose forms of pentoses.
History
EC 1.1.5.2 created 1982 as EC 1.1.99.17, transferred 2003 to EC 1.1.5.2, modified 2010
Pathway
ec00030  Pentose phosphate pathway
Orthology
K00117  quinoprotein glucose dehydrogenase
Genes
ECO: b0124(gcd)
ECJ: JW0120(gcd)
ECD: ECDH10B_0104(gcd)
EBW: BWG_0117(gcd)
ECOK: ECMDS42_0115(gcd)
ECE: Z0134(gcd)
ECS: ECs0128
ECF: ECH74115_0132(gcd)
ETW: ECSP_0125(gcd)
ELX: CDCO157_0126
EOJ: ECO26_0126(gcd)
EOI: ECO111_0125(gcd)
EOH: ECO103_0124(gcd)
ECOO: ECRM13514_0127(gcd)
ECOH: ECRM13516_0130(gcd)
ECG: E2348C_0127(gcd)
EOK: G2583_0128(gcd)
ESO: O3O_04440
ESM: O3M_20845
ESL: O3K_20945
ECW: EcE24377A_0126(gcd)
ELH: ETEC_0120
ECC: c0153(gcd)
ECP: ECP_0132
ECI: UTI89_C0137(gcd)
ECV: APECO1_1861(gcd)
ECX: EcHS_A0128(gcd)
ECM: EcSMS35_0134(gcd)
ECY: ECSE_0124
ECR: ECIAI1_0122(gcd)
ECQ: ECED1_0128(gcd)
ECK: EC55989_0117(gcd)
ECT: ECIAI39_0124(gcd)
EOC: CE10_0124(gcd)
EUM: ECUMN_0121(gcd)
ECZ: ECS88_0133(gcd)
ELO: EC042_0123(gcd)
ESE: ECSF_0137
EBR: ECB_00123(gcd)
EBD: ECBD_3495
EKF: KO11_00595(gcd)
EAB: ECABU_c01370(gcd)
EDJ: ECDH1ME8569_0118(gcd)
EIH: ECOK1_0126(gcd)
ELW: ECW_m0121(gcd)
ELL: WFL_00595(gcd)
ELC: i14_0140(gcd)
ELD: i02_0140(gcd)
EBL: ECD_00123(gcd)
EBE: B21_00122(gcd)
ELF: LF82_0815(gcd)
ECOI: ECOPMV1_00130(gcd)
ECOJ: P423_00665
ECOS: EC958_0266
EFE: EFER_0145(gcd)
EAL: EAKF1_ch1293(gcd)
STY: STY0191(gcd)
STT: t0174(gcd)
STM: STM0169(gcd)
SEO: STM14_0201(gcd)
SEY: SL1344_0170(gcd)
SEJ: STMUK_0171(gcd)
SEB: STM474_0178(gcd)
SEF: UMN798_0188(gcd)
SENR: STMDT2_01711(gcd)
SEND: DT104_01741(gcd)
SENI: CY43_00850
SPT: SPA0172(gcd)
SEK: SSPA0168
SEI: SPC_0182(gcd)
SEC: SCH_0169(gcd)
SEH: SeHA_C0193(gcd)
SHB: SU5_0811
SEE: SNSL254_A0185(gcd)
SEW: SeSA_A0188(gcd)
SEA: SeAg_B0201(gcd)
SENS: Q786_00895
SED: SeD_A0184(gcd)
SEL: SPUL_0185(gcd)
SEGA: SPUCDC_0185(gcd)
SET: SEN0174(gcd)
SENA: AU38_00865
SENO: AU37_00865
SENV: AU39_00865
SENQ: AU40_01010
SENL: IY59_00890
SEEP: I137_00825
SENB: BN855_1820(gcd)
SENE: IA1_00900
SBG: SBG_0161(gcd)
SBZ: A464_170
SFX: S0123(gcd)
SFV: SFV_0115(gcd)
SFE: SFxv_0127(gcd)
SFN: SFy_0158
SFS: SFyv_0162
SFT: NCTC1_00124(gcd)
SSN: SSON_0132(gcd)
SBO: SBO_0113(gcd)
ENC: ECL_00929
ECLO: ENC_46400
EEC: EcWSU1_00742(gcd)
ENF: AKI40_4156(gcd)
ESA: ESA_03208
CSK: ES15_3195(gcd)
CTU: CTU_07630(gcd)
KPN: KPN_00132(gcd)
KPU: KP1_0958(gcd)
KPP: A79E_4164
KPE: KPK_4605(gcd)
KPR: KPR_1061 KPR_1062(gcd)
KPJ: N559_4287
KPX: PMK1_02440(gcd)
KPNU: LI86_22050
KPNK: BN49_4208(gcd)
KVA: Kvar_4250
KOX: KOX_11135
KOE: A225_0936
EAE: EAE_11450
EAR: CCG31693
CKO: CKO_03243
CRO: ROD_01361(gcd)
CAMA: F384_00705
EBF: D782_3740
SRL: SOD_c29020(gcd)
SPLY: Q5A_016125(gcd)
SMAF: D781_2277
SMW: SMWW4_v1c31220(gcd)
SMAR: SM39_2583(gcd)
SMAC: SMDB11_2374(gcd)
SERF: L085_13040
RAA: Q7S_24406
ETA: ETA_23850(gcd)
EPY: EpC_25200(gcd)
EPR: EPYR_02730(gcd)
EAM: EAMY_1081(gcd)
EAY: EAM_1088(gcd)
EBI: EbC_12100(gcd) EbC_22470
ERJ: EJP617_22070(gcd)
EGE: EM595_1793(gcd1) EM595_3146(gcd2)
PAM: PANA_0312(gcd)
PLF: PANA5342_4100(gcd)
PAJ: PAJ_3473(gcd)
PVA: Pvag_1328(gcd1) Pvag_3575(gcd3)
PSTW: DSJ_03635
TPTY: NCTC11468_03349(gcd) NCTC11468_03630(sldA_1) NCTC11468_03631(sldA_2)
PMR: PMI1773(gcd)
PMIB: BB2000_1880(gcd)
XCC: XCC1575(gcd) XCC3083(gcd)
XCV: XCV1673(gcd1) XCV3337(gcd2)
XAX: XACM_1604(gcd)
XAC: XAC1633(gcd) XAC3212(gcd)
XCI: XCAW_03502(gcd)
XOR: XOC_3491
XPH: XppCFBP6546_18000(XppCFBP6546P_18000) XppCFBP6546_18465(XppCFBP6546P_18465)
SML: Smlt3136(gcd)
SMT: Smal_2577
SMZ: SMD_2716(gcd)
DKO: I596_930
PAE: PA2290(gcd)
PAEV: N297_2363
PAEI: N296_2363
PAU: PA14_34970(gcd)
PAP: PSPA7_2951(gcd)
PAG: PLES_30141(gcd)
PAF: PAM18_2750(gcd)
PNC: NCGM2_3301(gcd)
PAEB: NCGM1900_4239(gcd)
PAEP: PA1S_14170
PAEM: U769_13755
PAEL: T223_15400
PAEU: BN889_02498(gcd)
PAEG: AI22_19685
PAEC: M802_2360
PAEO: M801_2362
PMY: Pmen_0791
PMK: MDS_0905
PCQ: PcP3B5_43080(gcd)
PPU: PP_1444(gcd)
PPF: Pput_4277
PPT: PPS_4204
PPI: YSA_02756
PPX: T1E_2822
PPUT: L483_26210
PPUN: PP4_09940(gcd)
PMON: X969_20695
PMOT: X970_20330
PST: PSPTO_4196(gcd)
PSYR: N018_14495
PSP: PSPPH_3927(gcd)
PFL: PFL_4916(gcd)
PPRC: PFLCHA0_c48970(gdhA1)
PPRO: PPC_4926
PFO: Pfl01_4577(gcd)
PFS: PFLU_1086(gcd)
PFE: PSF113_4702(gcd)
PFC: PflA506_1058(gcd)
PFW: PF1751_v1c10390(gcd)
PFB: VO64_4211
PMAN: OU5_4692(gcd)
PEN: PSEEN1170
PPUU: PputUW4_00989(gdhA)
PSEM: TO66_25125
PSEC: CCOS191_4157(gdhA1)
PSOS: POS17_4889
PANR: A7J50_1088
PSIL: PMA3_24010
AVN: Avin_40050(gcd)
AVL: AvCA_40050(gcd)
AVD: AvCA6_40050(gcd)
ACX: Achr_10330(gcd)
PAR: Psyc_1237
PALI: A3K91_1117
PSYA: AOT82_235
ABM: ABSDF0596(gcd)
ABY: ABAYE0633(gcd) ABAYE1605(gdhB)
ABN: AB57_3351
ABAD: ABD1_19740(gdhB) ABD1_27930(gcd)
ACC: BDGL_001432(gdhB) BDGL_002309(gcd)
ACI: ACIAD2983(gcd)
ASJ: AsACE_CH02208(gcd)
ILO: IL0790(gcd)
PAT: Patl_2112
PIN: Ping_3086
NWA: Nwat_1271
GAI: IMCC3135_28435(gcd)
CSA: Csal_2831
HEL: HELO_4006(gcd)
SALN: SALB1_0713
BCT: GEM_3560
BUB: BW23_5775
BGP: BGL_2c12190(gcd)
BGU: KS03_4660
BGO: BM43_5051
BUO: BRPE64_DCDS01530(gcd)
BXB: DR64_3668(gcd) DR64_8255(gcd)
BPH: Bphy_5562
PLG: NCTC10937_01132(gcd)
BPT: Bpet4644(gcd)
BHO: D560_2070
BHM: D558_2053
BHZ: ACR54_04029(quiA_2)
ODI: ODI_R0130
AAV: Aave_0411
AAA: Acav_0472
DAC: Daci_0342
HYB: Q5W_06260
MPT: Mpe_A1594
RGE: RGE_36270(gcd)
MLO: mll1500
MES: Meso_3525
RBS: RHODOSMS8_01586(gcd)
SME: SMc00110(gcd)
SMX: SM11_chr0640(gcd1)
SMI: BN406_00638(gdh)
SMEL: SM2011_c00110(gcd)
SMER: DU99_05070
SMD: Smed_0595
SFH: SFHH103_00677(gcd)
SFD: USDA257_c07100(gdh)
SAME: SAMCFNEI73_Ch1051(gdh)
EAD: OV14_1978
ATU: Atu4135(gcd)
ARA: Arad_7145(gcd) Arad_9054(gcd)
ATF: Ach5_39120(gcd)
AVI: Avi_2843(gcd)
RET: RHE_CH01222(gcd)
REL: REMIM1_CH01225(gcd)
REP: IE4803_CH01249(gcd)
REI: IE4771_CH01292(gcd)
RLE: RL1354(gcd)
RIR: BN877_II1262(gcd)
RHL: LPU83_1205(gcd)
RGA: RGR602_CH01145(gcd)
RHN: AMJ98_CH01261(gcd)
RPHA: AMC79_CH01268(gcd)
RHT: NT26_2894(gcd) NT26_p10189(sldAB)
RHX: AMK02_CH01265(gcd)
RHK: Kim5_CH01373(gcd)
SHZ: shn_05260
OAN: Oant_0294
OAH: DR92_13
BRA: BRADO0601(gcd)
BBT: BBta_7581(gcd)
BRS: S23_24770
BRO: BRAD285_0066(gcd)
RPB: RPB_3211
RPT: Rpal_3825
VGO: GJW-30_1_02086(gcd)
MOR: MOC_1904
PHL: KKY_699
MMED: Mame_01372(gcd)
PZU: PHZ_c1591
RSP: RSP_2673
KVU: EIO_0680
KVL: KVU_0226(gcd)
CID: P73_4333
SPSE: SULPSESMR1_03550(sldA)
SPHP: LH20_10710
SGI: SGRAN_2352(sldA)
SPHM: G432_10700
STAX: MC45_12400
SSY: SLG_04410
SPMI: K663_04805
SPHR: BSY17_3937
BLAS: BSY18_2493
AAY: WYH_01145(quiA_1) WYH_01151(quiA_2) WYH_01157(quiA_3) WYH_01670(sldA)
GDI: GDI0325(gcd) GDI0539(gcd) GDI3277(gdhA)
ASZ: ASN_2518(gcd) ASN_2834(gcd)
RCE: RC1_3887(gcd)
AZL: AZL_e01560(gcd)
ALI: AZOLI_p50302(gcd)
TMO: TMO_1466(gdhA) TMO_1900(sldA) TMO_a0334
TXI: TH3_12430
PUB: SAR11_0305(yliI)
TTH: TT_C0202
OTE: Oter_0062
OBG: Verru16b_00210(gcd)
RBA: RB10127 RB1988(gdhP)
PLH: VT85_13575(gcd)
FMR: Fuma_01625(quiA)
SACI: Sinac_7278
PBOR: BSF38_04320(quiA)
ABAS: ACPOL_1581
ABAC: LuPra_00945(gcd_1) LuPra_01417(quiA_1) LuPra_01478(gcd_2) LuPra_04371(gcd_3) LuPra_05179(quiA_2)
GAU: GAU_2308
CPI: Cpin_2704
SMIZ: 4412673_03637(gcd)
MUC: MuYL_3275
MGOT: MgSA37_03285(gcd)
LBY: Lbys_1799
FAE: FAES_0550
MLT: VC82_1157
HMA: pNG7073(qgd)
 » show all
Taxonomy
Reference
1  [PMID:8509415]
  Authors
Yamada M, Sumi K, Matsushita K, Adachi O, Yamada Y.
  Title
Topological analysis of quinoprotein glucose dehydrogenase in Escherichia coli and its ubiquinone-binding site.
  Journal
J Biol Chem 268:12812-7 (1993)
  Sequence
[eco:b0124]
Reference
2  [PMID:9578566]
  Authors
Dewanti AR, Duine JA.
  Title
Reconstitution of membrane-integrated quinoprotein glucose dehydrogenase apoenzyme with PQQ and the holoenzyme's mechanism of action.
  Journal
Biochemistry 37:6810-8 (1998)
DOI:10.1021/bi9722610
Reference
3  [PMID:520586]
  Authors
Duine JA, Frank J, van Zeeland JK.
  Title
Glucose dehydrogenase from Acinetobacter calcoaceticus: a 'quinoprotein'.
  Journal
FEBS Lett 108:443-6 (1979)
DOI:10.1016/0014-5793(79)80584-0
Reference
4  [PMID:6793395]
  Authors
Ameyama M, Matsushita K, Ohno Y, Shinagawa E, Adachi O
  Title
Existence of a novel prosthetic group, PQQ, in membrane-bound, electron transport chain-linked, primary dehydrogenases of oxidative bacteria.
  Journal
FEBS Lett 130:179-83 (1981)
DOI:10.1016/0014-5793(81)81114-3
Reference
5  [PMID:8554505]
  Authors
Cozier GE, Anthony C
  Title
Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled  on that of methanol dehydrogenase from Methylobacterium extorquens.
  Journal
Biochem J 312 ( Pt 3):679-85 (1995)
  Sequence
[eco:b0124]
Reference
6  [PMID:10359647]
  Authors
Cozier GE, Salleh RA, Anthony C
  Title
Characterization of the membrane quinoprotein glucose dehydrogenase from Escherichia coli and characterization of a site-directed mutant in which histidine-262 has been changed to tyrosine.
  Journal
Biochem J 340 ( Pt 3):639-47 (1999)
  Sequence
[eco:b0124]
Reference
7  [PMID:11604400]
  Authors
Elias M, Tanaka M, Sakai M, Toyama H, Matsushita K, Adachi O, Yamada M.
  Title
C-terminal periplasmic domain of Escherichia coli quinoprotein glucose dehydrogenase transfers electrons to ubiquinone.
  Journal
J Biol Chem 276:48356-61 (2001)
DOI:10.1074/jbc.M107355200
  Sequence
[eco:b0124]
Reference
8  [PMID:12686133]
  Authors
James PL, Anthony C
  Title
The metal ion in the active site of the membrane glucose dehydrogenase of Escherichia coli.
  Journal
Biochim Biophys Acta 1647:200-5 (2003)
DOI:10.1016/S1570-9639(03)00041-4
  Sequence
[eco:b0124]
Reference
9  [PMID:14612441]
  Authors
Elias MD, Nakamura S, Migita CT, Miyoshi H, Toyama H, Matsushita K, Adachi O, Yamada M
  Title
Occurrence of a bound ubiquinone and its function in Escherichia coli membrane-bound quinoprotein glucose dehydrogenase.
  Journal
J Biol Chem 279:3078-83 (2004)
DOI:10.1074/jbc.M310163200
  Sequence
[eco:b0124]
Reference
10 [PMID:18550551]
  Authors
Mustafa G, Ishikawa Y, Kobayashi K, Migita CT, Elias MD, Nakamura S, Tagawa S, Yamada M
  Title
Amino acid residues interacting with both the bound quinone and coenzyme, pyrroloquinoline quinone, in Escherichia coli membrane-bound glucose dehydrogenase.
  Journal
J Biol Chem 283:22215-21 (2008)
DOI:10.1074/jbc.M800911200
  Sequence
[eco:b0124]
Other DBs
ExplorEnz - The Enzyme Database: 1.1.5.2
IUBMB Enzyme Nomenclature: 1.1.5.2
ExPASy - ENZYME nomenclature database: 1.1.5.2
BRENDA, the Enzyme Database: 1.1.5.2
CAS: 81669-60-5

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