KEGG   ENZYME: 1.1.2.8Help
Entry
EC 1.1.2.8                  Enzyme                                 

Name
alcohol dehydrogenase (cytochrome c);
type I quinoprotein alcohol dehydrogenase;
quinoprotein ethanol dehydrogenase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With a cytochrome as acceptor
BRITE hierarchy
Sysname
alcohol:cytochrome c oxidoreductase
Reaction(IUBMB)
a primary alcohol + 2 ferricytochrome c = an aldehyde + 2 ferrocytochrome c + 2 H+
Reaction(KEGG)
Substrate
primary alcohol [CPD:C00226];
ferricytochrome c [CPD:C00125]
Product
aldehyde [CPD:C00071];
ferrocytochrome c [CPD:C00126];
H+ [CPD:C00080]
Comment
A periplasmic PQQ-containing quinoprotein. Occurs in Pseudomonas and Rhodopseudomonas. The enzyme from Pseudomonas aeruginosa uses a specific inducible cytochrome c550 as electron acceptor. Acts on a wide range of primary and secondary alcohols, but not methanol. It has a homodimeric structure [contrasting with the heterotetrameric structure of EC 1.1.2.7, methanol dehydrogenase (cytochrome c)]. It is routinely assayed with phenazine methosulfate as electron acceptor. Activity is stimulated by ammonia or amines. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ.
History
EC 1.1.2.8 created 1972 as 1.1.99.8, modified 1982, part transferred 2010 to EC 1.1.2.8
Pathway
Glycolysis / Gluconeogenesis
Chloroalkane and chloroalkene degradation
Metabolic pathways
Biosynthesis of secondary metabolites
Microbial metabolism in diverse environments
Biosynthesis of antibiotics
Orthology
K00114  
alcohol dehydrogenase (cytochrome c)
Genes
PGE: 
SNJ: 
FAU: 
DTX: 
DKO: 
GHO: 
PAE: 
PA1982(exaA)
PAEV: 
N297_2045(exaA)
PAEI: 
N296_2045(exaA)
PAU: 
PAP: 
PAG: 
PAF: 
PNC: 
PAEB: 
PDK: 
PSG: 
PRP: 
PAEP: 
PAEM: 
PAEL: 
PAES: 
PAEU: 
PAEG: 
PAEC: 
M802_2043(exaA)
PAEO: 
M801_2044(exaA)
PMY: 
PMK: 
PRE: 
PPSE: 
PCQ: 
PPU: 
PP_2674(qedH-I) PP_2679(qedH-II)
PPF: 
PPG: 
PPT: 
PPB: 
PPI: 
PPX: 
PPUH: 
PPUT: 
PPUN: 
PP4_31590(pedH) PP4_31640(pedE)
PPUD: 
PMON: 
PMOT: 
PPJ: 
PFL: 
PFL_2216(pedE) PFL_2221(pedH)
PPRC: 
PPRO: 
PPC_2256(pedE) PPC_2261(pedH)
PFE: 
PFW: 
PFF: 
PMAN: 
PTV: 
PCG: 
PSA: 
PSZ: 
PSR: 
PSC: 
PSJ: 
PSH: 
PSTU: 
PBM: 
PBA: 
PBC: 
PPUU: 
PSK: 
PKC: 
PKB_2782(exaA)
PSW: 
PSOS: 
PFK: 
PBB: 
SWD: 
CPS: 
CPS_1887(exaA)
COLW: 
PAT: 
MHC: 
MARHY3265(exaA) MARHY3268(exaA)
MAD: 
MBS: 
MPQ: 
MARI: 
MLQ: 
MSQ: 
AMH: 
AMAA: 
AMAL: 
AMAE: 
AMAO: 
AMAD: 
AMAI: 
AMAG: 
AMAC: 
AMB: 
AMG: 
AMK: 
ALT: 
AAL: 
ASP: 
ASQ: 
GAG: 
CYQ: 
Q91_2236(exaA)
CZA: 
BLEP: 
NHL: 
AEH: 
HCS: 
HAK: 
ADI: 
APAC: 
AXE: 
MARS: 
SDF: 
GBI: 
PSPI: 
PSE: 
AQL: 
RPI: 
RPF: 
RPJ: 
RMN: 
RIN: 
REU: 
REH: 
H16_B1047(quiA)
CNC: 
CTI: 
CBW: 
CGD: 
CR3_1418(exaA)
CCUP: 
BVI: 
BVE: 
BCN: 
BCH: 
BCM: 
BCJ: 
BCEN: 
BCEW: 
BCEO: 
BAM: 
BAC: 
BMU: 
BMJ: 
BMK: 
BMUL: 
BCED: 
BCEP: 
BDL: 
BCON: 
BUB: 
BDF: 
BLAT: 
BTEI: 
BUG: 
BGE: 
BGF: 
BYI: 
BUK: 
BUO: 
BUE: 
BUQ: 
BXE: 
BXB: 
BPH: 
BPX: 
BFN: 
BCAI: 
PTX: 
AKA: 
AMIM: 
PNA: 
VAP: 
VPD: 
HYR: 
HYL: 
MPT: 
JAZ: 
JAL: 
LCH: 
THI: 
RGU: 
METR: 
RBU: 
DAR: 
AZO: 
azo2975(exaA3)
AZA: 
AZI: 
TMZ: 
THU: 
SULR: 
ANT: 
ALP: 
SMD: 
RHI: 
SFH: 
SFD: 
SIX: 
SHZ: 
BJA: 
blr6207(exaA)
BJU: 
BJP: 
BRA: 
BBT: 
BRS: 
AOL: 
BRC: 
BRAD: 
BIC: 
XAU: 
MEX: 
MEA: 
MDI: 
MCH: 
MRD: 
MET: 
MPO: 
MOR: 
META: 
MAQU: 
BID: 
MSL: 
HDN: 
HDT: 
HMC: 
HNI: 
PHL: 
DEQ: 
RHZ: 
MBRY: 
SIL: 
RCP: 
RHP: 
PAMI: 
DSH: 
Dshi_2673(exaA)
KVL: 
KRO: 
PGD: 
RHC: 
DON: 
TPRO: 
TOM: 
PABY: 
NAR: 
NPP: 
NRE: 
SWI: 
SMY: 
SJP: 
SYB: 
SPMI: 
SPHR: 
SINB: 
AAY: 
WYH_01154(qbdA_2)
CNA: 
PNS: 
GOX: 
GOH: 
GOY: 
GAL: 
GBE: 
ACR: 
AMV: 
GDI: 
GDI2040(adhA)
GDJ: 
GXY: 
GXL: 
KNA: 
APT: 
APW: 
APF: 
APU: 
APG: 
APQ: 
APX: 
APZ: 
APK: 
ASZ: 
ASN_1348(adhA) ASN_1383(adhA) ASN_1513(adhA)
ASV: 
AACE: 
APER: 
KBA: 
NCH: 
AZL: 
ALI: 
ABS: 
ABQ: 
ABF: 
ATI: 
PBD: 
PGM: 
PRI: 
DKU: 
MSM: 
MSG: 
MSB: 
MSN: 
MSH: 
MGO: 
SHY: 
SHO: 
NOA: 
GOB: 
SEN: 
SACE_4449(exaA)
AMQ: 
PDX: 
PSEA: 
PSEE: 
PSEH: 
PSEQ: 
PECQ: 
PHH: 
KPHY: 
DAB: 
TSA: 
TRS: 
SUS: 
ABAC: 
LuPra_00240(qbdA_1) LuPra_00349(qbdA_2) LuPra_02152(qgdA_2) LuPra_04749(qbdA_4)
HTH: 
HTE: 
NMV: 
NPE: 
TAA: 
CSU: 
 » show all
Taxonomy
Reference
1  [PMID:3144289]
  Authors
Rupp M, Gorisch H
  Title
Purification, crystallisation and characterization of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa.
  Journal
Biol. Chem. Hoppe. Seyler. 369 (1988) 431-9.
Reference
2  [PMID:7730276]
  Authors
Toyama H, Fujii A, Matsushita K, Shinagawa E, Ameyama M, Adachi O
  Title
Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols.
  Journal
J. Bacteriol. 177 (1995) 2442-50.
  Sequence
Reference
3  [PMID:10075429]
  Authors
Schobert M, Gorisch H
  Title
Cytochrome c550 is an essential component of the quinoprotein ethanol oxidation system in Pseudomonas aeruginosa: cloning and sequencing of the genes encoding cytochrome c550 and an adjacent acetaldehyde dehydrogenase.
  Journal
Microbiology. 145 ( Pt 2) (1999) 471-81.
  Sequence
[pae:PA1982]
Reference
4  [PMID:10736230]
  Authors
Keitel T, Diehl A, Knaute T, Stezowski JJ, Hohne W, Gorisch H
  Title
X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity.
  Journal
J. Mol. Biol. 297 (2000) 961-74.
  Sequence
[pae:PA1982]
Reference
5  [PMID:15094044]
  Authors
Kay CW, Mennenga B, Gorisch H, Bittl R
  Title
Characterisation of the PQQ cofactor radical in quinoprotein ethanol dehydrogenase of Pseudomonas aeruginosa by electron paramagnetic resonance spectroscopy.
  Journal
FEBS. Lett. 564 (2004) 69-72.
Reference
6  [PMID:19224199]
  Authors
Mennenga B, Kay CW, Gorisch H
  Title
Quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: the unusual disulfide ring formed by adjacent cysteine residues is essential for efficient electron transfer to cytochrome c550.
  Journal
Arch. Microbiol. 191 (2009) 361-7.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

DBGET integrated database retrieval system