| Entry |
|
|---|
| Name |
quinoprotein glucose dehydrogenase;
D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase;
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
 |
|---|
| Sysname |
D-glucose:ubiquinone oxidoreductase |
|---|
| Reaction(IUBMB) |
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
[RN:R06620] |
|---|
| Reaction(KEGG) |
R06620
 |
|---|
| Substrate |
D-glucose [CPD:C00031];
ubiquinone [CPD:C00399] |
|---|
| Product |
D-glucono-1,5-lactone [CPD:C00198];
ubiquinol [CPD:C00390] |
|---|
| Cofactor |
PQQ [CPD:C00113] |
|---|
| Comment |
Requires Mg2+ or Ca2+ for maximal activity. This is a PQQ-containing
quinoprotein that catalyses a direct oxidation of D-glucose to
D-gluconate in the periplasm of some bacteria and concomitantly
transfers electrons to ubiquinol oxidase through ubiquinone in the
respiratory chain. |
|---|
| Pathway |
PATH: ec00030 Pentose phosphate pathway
PATH: ec01100 Metabolic pathways |
|---|
| Orthology |
KO: K00117 quinoprotein glucose dehydrogenase |
|---|
| Genes |
ECO: b0124(gcd)
ECJ: JW0120(gcd)
ECD: ECDH10B_0104(gcd)
EBW: BWG_0117(gcd)
ECE: Z0134(gcd)
ECS: ECs0128
ECF: ECH74115_0132(gcd)
ETW: ECSP_0125(gcd)
ECG: E2348C_0127(gcd)
ECC: c0153(gcd)
ECI: UTI89_C0137(gcd)
ECP: ECP_0132
ECV: APECO1_1861(gcd)
ECW: EcE24377A_0126(gcd)
ECX: EcHS_A0128(gcd)
ECM: EcSMS35_0134(gcd)
ECY: ECSE_0124
ECL: EcolC_3535
ECK: EC55989_0117(gcd)
ECQ: ECED1_0128(gcd)
ECR: ECIAI1_0122(gcd)
ECT: ECIAI39_0124(gcd)
ECZ: ECS88_0133(gcd)
EUM: ECUMN_0121(gcd)
ELF: LF82_0815(gcd)
EBL: B21_00122(gcd)
EBD: ECBD_3495
EBR: ECB_00123(gcd)
EOH: ECO103_0124(gcd)
EOI: ECO111_0125(gcd)
EOJ: ECO26_0126(gcd)
EFE: EFER_0145(gcd)
STY: STY0191(gcd)
STT: t0174(gcd)
SPT: SPA0172(gcd)
SEK: SSPA0168
SPQ: SPAB_00208
SEI: SPC_0182(gcd)
SEC: SC0169(gcd)
SEH: SeHA_C0193(gcd)
SEE: SNSL254_A0185(gcd)
SEW: SeSA_A0188(gcd)
SEA: SeAg_B0201(gcd)
SED: SeD_A0184(gcd)
SET: SEN0174(gcd)
SES: SARI_02825
STM: STM0169(gcd)
SFL: SF0121(gcd)
SFX: S0123(gcd)
SFV: SFV_0115(gcd)
SSN: SSON_0132(gcd)
SBO: SBO_0113(gcd)
ETA: ETA_23850(gcd)
ENT: Ent638_0672
ESA: ESA_03208
CTU: Ctu_07630(gcd)
KPN: KPN_00132(gcd)
KPE: KPK_4605(gcd)
KPU: KP1_0958(gcd)
CKO: CKO_03243
SPE: Spro_3100
PMR: PMI1773(gcd)
XCC: XCC1575(gcd) XCC3083(gcd)
XCB: XC_1075 XC_2659
XCA: xccb100_1109(gcd) xccb100_2685(gcd)
XCV: XCV1673(gcd1) XCV3337(gcd2)
XAC: XAC1633(gcd) XAC3212(gcd)
SML: Smlt3136(gcd)
SMT: Smal_2577
PAE: PA2290(gcd)
PAU: PA14_34970(gcd)
PAP: PSPA7_2951(gcd)
PAG: PLES_30141(gcd)
PPU: PP_1444(gcd)
PPF: Pput_4277
PPG: PputGB1_4361
PPW: PputW619_1081 PputW619_2610
PST: PSPTO_4196(gcd)
PSB: Psyr_2574 Psyr_3930
PSP: PSPPH_3927(gcd)
PFL: PFL_4916
PFO: Pfl01_4577
PFS: PFLU1086(gcd)
PEN: PSEEN1170
PMY: Pmen_0791
PSA: PST_0991 PST_1455 PST_3741
AVN: Avin_40050(gcd)
PAR: Psyc_1237
PRW: PsycPRwf_1775
ACI: ACIAD2983(gcd)
ACB: A1S_1951 A1S_2847
ABM: ABSDF0596(gcd)
ABY: ABAYE0633(gcd) ABAYE1605(gdhB)
ABC: ACICU_02070 ACICU_03096
ABN: AB57_2293 AB57_3351
ABB: ABBFA_000614 ABBFA_001498
ILO: IL0790(gcd)
PAT: Patl_2112
PIN: Ping_3086
CSA: Csal_2831
MMW: Mmwyl1_0992
BXE: Bxe_A1505 Bxe_C0173
BPH: Bphy_5562
BPY: Bphyt_1682
BGL: bglu_2g12650
BPT: Bpet4644(gcd)
AAV: Aave_0411
DAC: Daci_0342
VAP: Vapar_5020
MPT: Mpe_A1594
HAR: HEAR0054
PUB: SAR11_0305(yliI)
MLO: mll1500
MES: Meso_3525
PLA: Plav_2593 Plav_3055
SME: SMc00110(gcd)
SMD: Smed_0595
ATU: Atu4135(gcd)
ATC: AGR_L_1436
ARA: Arad_7145(gcd) Arad_9054(gcd)
AVI: Avi_2843(gcd)
RET: RHE_CH01222(gcd)
REC: RHECIAT_CH0001309(gcd)
RLE: RL1354(gcd)
RLT: Rleg2_0856
RLG: Rleg_0980 Rleg_5965
RHI: NGR_c07380
OAN: Oant_0294
BRA: BRADO0601(gcd)
BBT: BBta_7581(gcd)
RPB: RPB_3211
RPT: Rpal_3825
MRD: Mrad2831_1527
PZU: PHZ_c1591
RSP: RSP_2673
RSH: Rsph17029_1330 Rsph17029_3539
RSQ: Rsph17025_1211 Rsph17025_3339
RSK: RSKD131_0987 RSKD131_4187
SWI: Swit_1054 Swit_1900 Swit_2024
GOX: GOX0265 GOX0516 GOX0854 GOX1441
GDI: GDI_0325(gcd) GDI_0539(gcd) GDI_3277(gdhA)
GDJ: Gdia_1469 Gdia_2382 Gdia_3089
APT: APA01_06330 APA01_14620
RCE: RC1_3887(gcd)
SUS: Acid_1044 Acid_1183 Acid_1639 Acid_1932 Acid_2289 Acid_2557
Acid_3097 Acid_3236 Acid_4075 Acid_4918
DFE: Dfer_0311 Dfer_1014 Dfer_1378 Dfer_1611 Dfer_4957
CPI: Cpin_2704
GFO: GFO_0814(gdhB)
RBI: RB2501_06935
OTE: Oter_0062
GAU: GAU_2308
RBA: RB10127 RB1988(gdhP)
SYN: slr1608(gdhB)
TTH: TTC0202
HMA: pNG7073(qgd)
 |
|---|
Reference
Authors
Title
Journal
|
1
Ameyama, M., Nonobe, M., Hayashi, M., Shinagawa, E., Matsushita, K.
and Adachi, O.
Mode of binding of pyrroloquinoline quinone to apo-glucose
dehydrogenase.
Agric. Biol. Chem. 49 (1985) 1227-1231. |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:520586]
Duine JA, Frank J, van Zeeland JK.
Glucose dehydrogenase from Acinetobacter calcoaceticus: a
'quinoprotein'.
FEBS. Lett. 108 (1979) 443-6.
Acinetobacter calcoaceticus |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:8509415]
Yamada M, Sumi K, Matsushita K, Adachi O, Yamada Y.
Topological analysis of quinoprotein glucose dehydrogenase in
Escherichia coli and its ubiquinone-binding site.
J. Biol. Chem. 268 (1993) 12812-7.
Escherichia coli [GN:eco] |
|---|
Reference
Authors
Title
Journal
Organism
|
4 [PMID:9578566]
Dewanti AR, Duine JA.
Reconstitution of membrane-integrated quinoprotein glucose
dehydrogenase apoenzyme with PQQ and the holoenzyme's mechanism of
action.
Biochemistry. 37 (1998) 6810-8.
Acinetobacter calcoaceticus |
|---|
Reference
Authors
Title
Journal
Organism
|
5 [PMID:10518528]
Oubrie A, Rozeboom HJ, Dijkstra BW.
Active-site structure of the soluble quinoprotein glucose
dehydrogenase complexed with methylhydrazine: a covalent
cofactor-inhibitor complex.
Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 11787-91.
Acinetobacter calcoaceticus |
|---|
Reference
Authors
Title
Journal
Organism
|
6 [PMID:11604400]
Elias M, Tanaka M, Sakai M, Toyama H, Matsushita K, Adachi O, Yamada
M.
C-terminal periplasmic domain of Escherichia coli quinoprotein
glucose dehydrogenase transfers electrons to ubiquinone.
J. Biol. Chem. 276 (2001) 48356-61.
Escherichia coli [GN:eco] |
|---|
| 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 |
|---|
