KEGG   ENZYME: 1.3.3.11Help
Entry
EC 1.3.3.11                 Enzyme                                 

Name pyrroloquinoline-quinone synthase;
PqqC;
6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,5,6,7,8-
octahydroquinoline-2,4-dicarboxylate:oxygen oxidoreductase
(cyclizing) [incorrect]
Class Oxidoreductases;
Acting on the CH-CH group of donors;
With oxygen as acceptor
BRITE hierarchy
Sysname 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-
2,4-dicarboxylate:oxygen oxidoreductase (cyclizing)
Reaction(IUBMB) 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-
2,4-dicarboxylate + 3 O2 =
4,5-dioxo-4,5-dihydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-
tricarboxylate + 2 H2O2 + 2 H2O [RN:R07353]
Reaction(KEGG) R07353
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Substrate 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-
2,4-dicarboxylate [CPD:C15599];
O2 [CPD:C00007]
Product 4,5-dioxo-4,5-dihydro-1H-pyrrolo[2,3-f]quinoline-2,7,9-
tricarboxylate [CPD:C00113];
H2O2 [CPD:C00027];
H2O [CPD:C00001]
Comment So far only a single turnover of the enzyme has been observed, and
the pyrroloquinoline quinone remains bound to it. It is not yet
known what releases the product in the bacterium.
Orthology KO: K06137  pyrroloquinoline-quinone synthase
Genes ETA: ETA_28880(pqqC)
ESA: ESA_02994
CTU: Ctu_08720(pqqC)
KPN: KPN_01811
KPE: KPK_2543(pqqC)
KPU: KP1_2862(pqqC)
XCC: XCC2938(pqqC)
XCB: XC_1171
XCA: xccb100_1214
XCV: XCV3246(pqqC)
XAC: XAC3115(pqqC)
XOO: XOO1734(pqqC)
XOM: XOO_1635
XOP: PXO_01590(pqqC)
PAE: PA1987(pqqC)
PAU: PA14_38800(pqqC)
PAP: PSPA7_3307(pqqC)
PAG: PLES_33361(pqqC)
PPU: PP_0378(pqqC)
PPF: Pput_0403
PPG: PputGB1_0407
PPW: PputW619_4825
PST: PSPTO_0511(pqqC)
PSB: Psyr_4672
PSP: PSPPH_4706(pqqC)
PFL: PFL_5675
PFO: Pfl01_5159
PFS: PFLU5600(pqqC)
PEN: PSEEN0396(pqqC)
PMY: Pmen_1967
PSA: PST_2074(pqqC)
AVN: Avin_41660(pqqC)
ACI: ACIAD2505(pqqC)
ABM: ABSDF1981(pqqC)
ABY: ABAYE1880(pqqC)
ABC: ACICU_01796
ABN: AB57_1990(pqqC)
ABB: ABBFA_001733(pqqC)
SWD: Swoo_2251
CPS: CPS_0859(pqqC)
MCA: MCA1447(pqqC)
NOC: Noc_2621
CSA: Csal_0846
RPI: Rpic_0290 Rpic_2490
RPF: Rpic12D_2096
REU: Reut_A1780 Reut_B3762
REH: H16_B1051(pqqC1) H16_B1880(pqqC2)
RME: Rmet_3633
CTI: RALTA_A1791 RALTA_B0440(pqqC2) RALTA_B0670(pqqC1) RALTA_B1579
BVI: Bcep1808_6556
BCN: Bcen_3247
BCH: Bcen2424_5121
BCM: Bcenmc03_5160
BCJ: BCAM2362(pqqC)
BAM: Bamb_6166
BAC: BamMC406_5899
BMU: Bmul_5967
BMJ: BMULJ_05559(pqqC)
BXE: Bxe_A1825 Bxe_B2468(pqqC)
BPH: Bphy_6510
BGL: bglu_1g23050 bglu_2g05730 bglu_2g11480 bglu_2g22320
BPE: BP0359
BPA: BPP4174
BBR: BB4644
PNA: Pnap_0731
VEI: Veis_4036
VAP: Vapar_3055
MPT: Mpe_A2586
LCH: Lcho_0246 Lcho_4350
NEU: NE1434
NET: Neut_1553
NMU: Nmul_A2636
AZO: azo1188(pqqC)
DAR: Daro_1700
MFA: Mfla_1682
MMB: Mmol_0995
MEI: Msip34_1527
HOH: Hoch_6173
RFE: RF_0036
WOL: WD0880
WRI: WRi_008640
WPI: WPa_0697
NSE: NSE_0493(pqqC)
NRI: NRI_0466
SME: SM_b20206(pqqC)
SMD: Smed_3917
ARA: Arad_8717(pqqC)
RHI: NGR_b03280
BJA: blr6737(pqqC)
BRA: BRADO5795(pqqC)
BBT: BBta_6302(pqqC)
RPA: RPA1948(pqqC)
RPB: RPB_3421
RPC: RPC_0881
RPD: RPD_2031
RPE: RPE_0845
RPT: Rpal_2159
NWI: Nwi_0691
XAU: Xaut_1801
MET: M446_5766
MNO: Mnod_5990
BID: Bind_3321
MSL: Msil_1149 Msil_1739
SIL: SPO1502(pqqC)
RSP: RSP_0792(pqqC)
RSH: Rsph17029_2448
RSQ: Rsph17025_0388
RSK: RSKD131_2154
RDE: RD1_1152(pqqC)
PDE: Pden_2361
DSH: Dshi_0452(pqqC)
GOX: GOX0985
GBE: GbCGDNIH1_1928
ACR: Acry_0079 Acry_0323
GDI: GDI_1269(pqqC)
GDJ: Gdia_1980
APT: APA01_21270(pqqC)
AAC: Aaci_2183
MSM: MSMEG_1458 MSMEG_3723(pqqC)
MVA: Mvan_1325
RHA: RHA1_ro04372
ROP: ROP_42770
NCA: Noca_4284
FRA: Francci3_1999
SEN: SACE_4446(pqqC)
RXY: Rxyl_2551
CTR: CT610
CTA: CTA_0663(pqqC)
CTB: CTL0874
CTL: CTLon_0868
CTJ: JALI_6141
CMU: TC0900
CPN: CPn0761
CPA: CP1111
CPJ: CPj0761
CPT: CpB0789
CCA: CCA00996
CAB: CAB966
CFE: CF0017(pqqC)
ABA: Acid345_0078
ACA: ACP_2023
MIN: Minf_1235
NPU: Npun_R4837
TER: Tery_0845
AMR: AM1_4800
TAC: Ta0939
SSO: SSO2700
STO: ST2606
SAI: Saci_2243
SIS: LS215_2777
SIA: M1425_2616
SIM: M1627_2669
SID: M164_2601
SIY: YG5714_2788
SIN: YN1551_2977
MSE: Msed_0987
CMA: Cmaq_0589
NMR: Nmar_0288
Taxonomy
Reference
  Authors
  Title

  Journal
  Organism
1  [PMID:15113189]
Magnusson OT, Toyama H, Saeki M, Schwarzenbacher R, Klinman JP.
The structure of a biosynthetic intermediate of pyrroloquinoline
quinone (PQQ) and elucidation of the final step of PQQ biosynthesis.
J. Am. Chem. Soc. 126 (2004) 5342-3.
Klebsiella pneumoniae, Methylobacterium extorquens
Reference
  Authors

  Title

  Journal
  Organism
2  [PMID:15148379]
Magnusson OT, Toyama H, Saeki M, Rojas A, Reed JC, Liddington RC,
Klinman JP, Schwarzenbacher R.
Quinone biogenesis: Structure and mechanism of PqqC, the final
catalyst in the production of pyrroloquinoline quinone.
Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 7913-8.
Klebsiella pneumoniae, Methylobacterium extorquens [GN:mea]
Reference
  Authors
  Title


  Journal
  Organism
3  [PMID:9043136]
Toyama H, Chistoserdova L, Lidstrom ME.
Sequence analysis of pqq genes required for biosynthesis of
pyrroloquinoline quinone in Methylobacterium extorquens AM1 and the
purification of a biosynthetic intermediate.
Microbiology. 143 ( Pt 2) (1997) 595-602.
Klebsiella pneumoniae, Methylobacterium extorquens [GN:mea]
Reference
  Authors
  Title

  Journal
4  [PMID:1243798]
Yasunaga K.
[Concept of thrombocytopathy and problems involved in its diagnosis
(author's transl)]
Nippon. Ketsueki. Gakkai. Zasshi. 38 (1975) 734-40.
Reference
  Authors

  Title

  Journal
  Organism
5  [PMID:15211525]
Schwarzenbacher R, Stenner-Liewen F, Liewen H, Reed JC, Liddington
RC.
Crystal structure of PqqC from Klebsiella pneumoniae at 2.1 A
resolution.
Proteins. 56 (2004) 401-3.
Klebsiella pneumoniae
Other DBs ExplorEnz - The Enzyme Database: 1.3.3.11
IUBMB Enzyme Nomenclature: 1.3.3.11
ExPASy - ENZYME nomenclature database: 1.3.3.11
BRENDA, the Enzyme Database: 1.3.3.11
CAS: 353484-42-1

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