KEGG   ENZYME: 1.1.2.8
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
Sysname
alcohol:cytochrome c oxidoreductase
Reaction(IUBMB)
a primary alcohol + 2 ferricytochrome c = an aldehyde + 2 ferrocytochrome c + 2 H+
Reaction(KEGG)
(other) R05062 R05198 R05285
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
Orthology
K00114  alcohol dehydrogenase (cytochrome c)
Genes
DTX: ATSB10_32210
DKO: I596_887
RBD: ALSL_0372
GHO: AL542_11380 AL542_17210
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)
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)
PCQ: PcP3B5_36440(qedA) PcP3B5_36490(exaA)
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)
PPRO: PPC_2256(pedE) PPC_2261(pedH)
PKC: PKB_2782(exaA)
PSOS: POS17_2165(pedE) POS17_2170(pedH)
SWD: Swoo_2255
CPS: CPS_1887(exaA)
PAT: Patl_1855
MHC: MARHY3265(exaA) MARHY3268(exaA)
MBS: MRBBS_1203(exaA)
MARJ: MARI_32520(qedA) MARI_32550(exaA)
AMAL: I607_15570
AMAE: I876_15870
AMAO: I634_15815
AMAD: I636_15730
AMAI: I635_16370
AMAG: I533_15455
ASP: AOR13_207
MEJ: Q7A_2587
MEC: Q7C_1053
CYQ: Q91_2236(exaA)
CZA: CYCME_2554(exaA)
AEH: Mlg_2729
GAI: IMCC3135_20825(qedA)
HOL: HORIV_65430(exaA)
ADI: B5T_01640
APAC: S7S_07215
AXE: P40_07725
PSE: NH8B_3445
RPI: Rpic_2494
REH: H16_B1047(quiA)
CNC: CNE_1c16910(exaA) CNE_2c10080(quiA)
CTI: RALTA_B0666(exaA2)
CGD: CR3_1418(exaA)
BVE: AK36_5998
BCN: Bcen_3242
BCJ: BCAM2368
BCEN: DM39_5476
BCEW: DM40_5672
BCEO: I35_6264
BAM: Bamb_6162
BMU: Bmul_5972
BMK: DM80_6422
BMUL: NP80_5666
BCED: DM42_5620
BDL: AK34_5438
BCON: NL30_00625
BUB: BW23_3523
BLAT: WK25_18580
BTEI: WS51_29325
BSEM: WJ12_31775
BPSL: WS57_02270
BMEC: WJ16_30215
BUK: MYA_5958
BXE: Bxe_B0306
BPH: Bphy_7192
BFN: OI25_3470
CABA: SBC2_61100(qbdA)
AMIM: MIM_c02340(qheDH2) MIM_c11110
PNA: Pnap_0726
VEI: Veis_4951
HPSE: HPF_00420(qbdA) HPF_17540(qedA)
THI: THI_0488
MMB: Mmol_1214
DAR: Daro_1023
AZO: azo2975(exaA3)
SULR: B649_05170
PACO: AACT_0601
SFH: SFHH103_06439(exaA)
SFD: USDA257_c26010(exaA)
SHZ: shn_29600
BJA: blr6207(exaA)
BRA: BRADO5480
BBT: BBta_5964
BRS: S23_20730 S23_20880(exaA)
MEA: Mex_1p1139(exa)
MDI: METDI1985(exa)
MCH: Mchl_1540
MPO: Mpop_4873
MET: M446_3624
META: Y590_05690
SIL: SPO1508
RUT: FIU92_21330(qedA)
RCP: RCAP_rcc01396(exaA1) RCAP_rcc01657(exaA2)
DSH: Dshi_2673(exaA)
PGD: Gal_03916
LAQU: R2C4_20155
RHC: RGUI_2633
ROH: FIU89_03675(qedA)
AHT: ANTHELSMS3_00910(exaA)
MARU: FIU81_10580(qedA)
ROT: FIV09_16890(qedA)
MALU: KU6B_53540
SWI: Swit_0693
SPHD: HY78_23230
SECH: B18_21810
SPMI: K663_19553
SINB: SIDU_18365
SPHT: K426_25214
AAY: WYH_01154(qbdA_2)
ALB: AEB_P3030
APK: APA386B_1070(adhA)
ASZ: ASN_1348(adhA)
AFR: AFE_1981
PRI: PRIO_3756
SHY: SHJG_2432
GOB: Gobs_2451
SEN: SACE_4449(exaA)
AMQ: AMETH_4524(exaA)
PDX: Psed_0735
PSEA: WY02_27590
PSEH: XF36_14225
PAUT: Pdca_29050
AFS: AFR_41200
DGE: Dgeo_1149
DFC: DFI_15370
RBA: RB12303
PBAS: SMSP2_00328(qgdA)
ABAC: LuPra_00240(qbdA_1) LuPra_00349(qbdA_2) LuPra_02152(qgdA_2) LuPra_04749(qbdA_4)
NMV: NITMOv2_2763(adh)
HTU: Htur_0673
NMG: Nmag_0742
TAA: NMY3_03104(adhA)
NFN: NFRAN_0518(adhA)
 » show all
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)
DOI:10.1515/bchm3.1988.369.1.431
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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