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 1.1.99.17, transferred 2003 to EC 1.1.5.2, modified 2010
Pathway
Pentose phosphate pathway
Orthology
K00117  
quinoprotein glucose dehydrogenase
Genes
ECO: 
b0124(gcd)
ECJ: 
ECD: 
EBW: 
ECOK: 
ECE: 
Z0134(gcd)
ECS: 
ECF: 
ETW: 
ELX: 
EOJ: 
EOI: 
EOH: 
ECG: 
EOK: 
ELR: 
ECC: 
c0153(gcd)
ECP: 
ECI: 
ECV: 
ECX: 
ECW: 
ECM: 
ECY: 
ECR: 
ECQ: 
ECK: 
ECT: 
EOC: 
EUM: 
ECZ: 
ELO: 
ELN: 
ELH: 
ESE: 
ESO: 
ESM: 
ESL: 
ECL: 
EBR: 
EBD: 
EKO: 
EKF: 
EAB: 
EDH: 
EDJ: 
EIH: 
ENA: 
ELU: 
EUN: 
ELW: 
ELL: 
ELC: 
ELD: 
EBL: 
EBE: 
ELF: 
ECOA: 
ECOL: 
ECOI: 
ECOJ: 
EFE: 
STY: 
STY0191(gcd)
STT: 
t0174(gcd)
SEX: 
SENT: 
STM: 
STM0169(gcd)
SEO: 
SEV: 
SEY: 
SEM: 
SEJ: 
SEB: 
SEF: 
SETU: 
SETC: 
SEEN: 
SENR: 
SEND: 
SPT: 
SPA0172(gcd)
SEK: 
SPQ: 
SEI: 
SEC: 
SC0169(gcd)
SEH: 
SHB: 
SENH: 
SEEH: 
SEE: 
SENN: 
SEW: 
SEA: 
SENS: 
SED: 
SEL: 
SEGA: 
SET: 
SEN0174(gcd)
SENJ: 
SEEC: 
SEEB: 
SEEP: 
SENB: 
BN855_1820(SBOV01311)
SENE: 
SES: 
SBG: 
SBZ: 
SFX: 
S0123(gcd)
SFV: 
SFE: 
SSN: 
SSJ: 
SBO: 
SDZ: 
ETA: 
EPY: 
EPR: 
EAM: 
EAY: 
EBI: 
ERJ: 
ENT: 
ENC: 
ENO: 
ECLO: 
ESC: 
EEC: 
ENL: 
EAS: 
EAE: 
EAR: 
ENR: 
ESA: 
CSK: 
CSZ: 
CSI: 
CTU: 
KPN: 
KPU: 
KPM: 
KPP: 
KPE: 
KPO: 
KPR: 
KPJ: 
KPI: 
KVA: 
KOX: 
KOE: 
CKO: 
CRO: 
SPE: 
SRR: 
SRL: 
SRY: 
SRS: 
SRA: 
SMAF: 
SMW: 
SLQ: 
PMR: 
PMI1773(gcd)
PMIB: 
PAM: 
PLF: 
PAJ: 
PAQ: 
PVA: 
Pvag_1328(gcd1) Pvag_3575(gcd3)
PAO: 
RAH: 
RAQ: 
RAA: 
ROR: 
EBF: 
XCC: 
XCC1575(gcd) XCC3083(gcd)
XCB: 
XCA: 
XCV: 
XCV1673(gcd1) XCV3337(gcd2)
XCP: 
XAC: 
XAC1633(gcd) XAC3212(gcd)
XAX: 
XAO: 
XOR: 
XCI: 
SML: 
SMT: 
BUJ: 
SMZ: 
FAU: 
PAE: 
PA2290(gcd)
PAU: 
PAP: 
PAG: 
PAF: 
PNC: 
PDK: 
PSG: 
PRP: 
PAEP: 
PAER: 
PAEM: 
PAEL: 
PAES: 
PPU: 
PP_1444(gcd)
PPF: 
PPG: 
PPW: 
PPT: 
PPB: 
PPI: 
PPX: 
PPUH: 
PPUT: 
PPUN: 
PPUU: 
PST: 
PSB: 
PSP: 
PCI: 
PFL: 
PPRC: 
PFO: 
PFS: 
PFE: 
PFC: 
PPZ: 
PEN: 
PMY: 
PMK: 
PSA: 
PSZ: 
PSR: 
PSC: 
PSJ: 
PSH: 
PBA: 
PFV: 
PSV: 
PSK: 
PMON: 
PMOT: 
AVN: 
AVL: 
AVD: 
PAR: 
PRW: 
PSO: 
ACI: 
ACD: 
ACB: 
ABM: 
ABY: 
ABAYE0633(gcd) ABAYE1605(gdhB)
ABC: 
ABN: 
ABB: 
ABX: 
ABZ: 
ABR: 
ABD: 
ABH: 
ABAD: 
ABJ: 
ABAB: 
ABAJ: 
ABAZ: 
ACC: 
ILO: 
IL0790(gcd)
ILI: 
PAT: 
GAG: 
PIN: 
NWA: 
CSA: 
HEL: 
ADI: 
MMW: 
BCT: 
BXE: 
BPH: 
BPY: 
BGL: 
BUG: 
BGE: 
BGF: 
BGD: 
BYI: 
BPX: 
BUO: 
BPT: 
AKA: 
AAV: 
AAA: 
DAC: 
DEL: 
VAP: 
VPE: 
VPD: 
MPT: 
RGE: 
MLO: 
MCI: 
MOP: 
MAM: 
MES: 
PLA: 
SME: 
SMK: 
SMQ: 
SMX: 
SMI: 
SMEG: 
SMEL: 
SMD: 
RHI: 
SFH: 
SFD: 
ATU: 
Atu4135(gcd)
ARA: 
AVI: 
AGR: 
RET: 
REC: 
REL: 
RLE: 
RL1354(gcd)
RLT: 
RLG: 
RTR: 
RIR: 
OAN: 
BJU: 
BRA: 
BBT: 
BRS: 
RPB: 
RPT: 
RPX: 
AOL: 
MRD: 
HNI: 
PHL: 
PZU: 
RSP: 
RSH: 
RSQ: 
RSK: 
KVU: 
KVL: 
NPP: 
SWI: 
SPHM: 
SJP: 
SCH: 
SSY: 
GOX: 
GOH: 
GDI: 
GDI_0325(gcd) GDI_0539(gcd) GDI_3277(gdhA)
GDJ: 
GXY: 
APT: 
APW: 
APF: 
APU: 
APG: 
APQ: 
APX: 
APZ: 
APK: 
RCE: 
AZL: 
ALI: 
TMO: 
PUB: 
APM: 
OTE: 
GMA: 
TSA: 
TRS: 
SUS: 
GAU: 
RBA: 
SACI: 
CPI: 
SHG: 
HHY: 
CMR: 
DFE: 
SLI: 
LBY: 
RSI: 
EOL: 
FAE: 
GFO: 
GFO_0814(gdhB)
RBI: 
FBC: 
ZGA: 
MRS: 
TTH: 
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 (1993) 12812-7.
  Organism
Escherichia coli [GN:eco]
  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 (1998) 6810-8.
  Organism
Acinetobacter calcoaceticus
Reference
3  [PMID:520586]
  Authors
Duine JA, Frank J, van Zeeland JK.
  Title
Glucose dehydrogenase from Acinetobacter calcoaceticus: a 'quinoprotein'.
  Journal
FEBS. Lett. 108 (1979) 443-6.
  Organism
Acinetobacter calcoaceticus
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 (1981) 179-83.
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) (1995) 679-85.
  Organism
Escherichia coli [GN:eco]
  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) (1999) 639-47.
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 (2001) 48356-61.
  Organism
Escherichia coli [GN:eco]
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 (2003) 200-5.
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 (2004) 3078-83.
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 (2008) 22215-21.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
81669-60-5

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