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 EC 1.1.99.8, modified 1982, part transferred 2010 to EC 1.1.2.8
Pathway
ec00010  Glycolysis / Gluconeogenesis
ec00625  Chloroalkane and chloroalkene degradation
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
ec01120  Microbial metabolism in diverse environments
ec01130  Biosynthesis of antibiotics
Orthology
K00114  alcohol dehydrogenase (cytochrome c)
Genes
PAE: PA1982(exaA)
PAEV: N297_2045(exaA)
PAEI: N296_2045(exaA)
PAU: PA14_38860(exaA)
PAP: PSPA7_3312(exaA)
PAG: PLES_33401(exaA)
PAF: PAM18_3063(exaA)
PNC: NCGM2_2955(exaA)
PAEB: NCGM1900_4505(exaA)
PDK: PADK2_15740
PAEP: PA1S_15785
PAEM: U769_15365
PAEL: T223_17060
PAEU: BN889_02154(exaA)
PAEG: AI22_17990
PAEC: M802_2043(exaA)
PAEO: M801_2044(exaA)
PRE: PCA10_31340(pedH) PCA10_31390(pedE)
PPU: PP_2674(qedH-I) PP_2679(qedH-II)
PPX: T1E_2678(exaA) T1E_2683
PPUN: PP4_31590(pedH) PP4_31640(pedE)
PFL: PFL_2216(pedE) PFL_2221(pedH)
PPRC: PFLCHA0_c22780(exaA1) PFLCHA0_c22820(exaA2)
SWD: Swoo_2255
CPS: CPS_1887(exaA)
PAT: Patl_1855
MHC: MARHY3265(exaA) MARHY3268(exaA)
MBS: MRBBS_1203(exaA)
AMAL: I607_15570
AMAE: I876_15870
AMAO: I634_15815
AMAD: I636_15730
AMAI: I635_16370
AMAG: I533_15455
CYQ: Q91_2236(exaA)
CZA: CYCME_2554(exaA)
NHL: Nhal_3866
AEH: Mlg_2729
ADI: B5T_01640
PSE: NH8B_3445
RPI: Rpic_2494
REH: H16_B1047(quiA)
CNC: CNE_2c10080(quiA)
CTI: RALTA_B0666(exaA2)
BCN: Bcen_3242
BCJ: BCAM2368
BAM: Bamb_6162
BMU: Bmul_5972
BUK: MYA_5958
BXE: Bxe_B0306
BPH: Bphy_7192
PNA: Pnap_0726
MPT: Mpe_A0473
LCH: Lcho_1811
THI: THI_0488
DAR: Daro_1023
AZO: azo2975(exaA3)
AZA: AZKH_1557
SULR: B649_05170
SMD: Smed_6351
SFH: SFHH103_06439(exaA)
SFD: USDA257_c26010(exaA)
BJA: blr6207(exaA)
BRA: BRADO5480
BBT: BBta_5964
BRS: S23_20880(exaA)
AOL: S58_22280
XAU: Xaut_1781
MEX: Mext_1339
MEA: Mex_1p1139(exa)
MDI: METDI1985(exa)
MCH: Mchl_1540
MPO: Mpop_4873
MET: M446_3624
BID: Bind_3639
MSL: Msil_3387
HDN: Hden_0340
SIL: SPO1508
RCP: RCAP_rcc01396(exaA1) RCAP_rcc01657(exaA2)
DSH: Dshi_2673(exaA)
SWI: Swit_0693
ACR: Acry_1741
SHY: SHJG_2432
GOB: Gobs_2451
SEN: SACE_4449(exaA)
PDX: Psed_0735
HTH: HTH_0392
 » 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 369:431-9 (1988)
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 177:2442-50 (1995)
DOI:10.1128/JB.177.9.2442-2450.1995
  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):471-81 (1999)
DOI:10.1099/13500872-145-2-471
  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 297:961-74 (2000)
DOI:10.1006/jmbi.2000.3603
  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 564:69-72 (2004)
DOI:10.1016/S0014-5793(04)00317-5
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 191:361-7 (2009)
DOI:10.1007/s00203-009-0460-4
Other DBs
ExplorEnz - The Enzyme Database: 1.1.2.8
IUBMB Enzyme Nomenclature: 1.1.2.8
ExPASy - ENZYME nomenclature database: 1.1.2.8
BRENDA, the Enzyme Database: 1.1.2.8

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