KEGG   ENZYME: 1.1.9.1Help
Entry
EC 1.1.9.1                  Enzyme                                 

Name
alcohol dehydrogenase (azurin);
type II quinoprotein alcohol dehydrogenase;
quinohaemoprotein ethanol dehydrogenase;
QHEDH;
ADHIIB
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With a copper protein as acceptor
BRITE hierarchy
Sysname
alcohol:azurin oxidoreductase
Reaction(IUBMB)
a primary alcohol + azurin = an aldehyde + reduced azurin [RN:R09480]
Reaction(KEGG)
Substrate
primary alcohol [CPD:C00226];
azurin
Product
aldehyde [CPD:C00071];
reduced azurin [CPD:C05358]
Comment
A soluble, periplasmic PQQ-containing quinohemoprotein. Also contains a single heme c. Occurs in Comamonas and Pseudomonas. Does not require an amine activator. Oxidizes a wide range of primary and secondary alcohols, and also aldehydes and large substrates such as sterols; methanol is not a substrate. Usually assayed with phenazine methosulfate or ferricyanide. 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 1.1.9.1 created 2010 as EC 1.1.98.1; transferred 2011 to EC 1.1.9.1
Orthology
K17760  quinohemoprotein ethanol dehydrogenase
Genes
PMK: MDS_2680
PCQ: PcP3B5_33080(qgdA_1)
PPW: PputW619_2696
PSZ: PSTAB_2905
PSR: PSTAA_3020
PSH: Psest_1423
PSTU: UIB01_10105
PSTT: CH92_09640
PBM: CL52_14245
PSK: U771_15535
GPS: C427_3776
ADI: B5T_04379(exaA1)
AXE: P40_21330
REH: H16_A1884(h16_A1884)
CNC: CNE_1c18660(qheDH) CNE_BB1p04310(adh)
CTI: RALTA_A1577(exaA1)
AMIM: MIM_c00090(qheDH1)
POL: Bpro_5302
VEI: Veis_0427
DAC: Daci_3352
CTES: O987_00960
HYB: Q5W_16030
PBH: AAW51_3568(qheDH)
AZO: azo3022(exaA4)
PLA: Plav_1306
RBS: RHODOSMS8_03066(qbdA)
BBT: BBta_5502
RPA: RPA3188
RPB: RPB_2355
RPD: RPD_3110
RPE: RPE_3525
RPT: Rpal_3601
VGO: GJW-30_1_04338(qheDH)
HMC: HYPMC_4861(adh)
RBM: TEF_09160
PZU: PHZ_c3112
KVL: KVU_0632
KRO: BVG79_00894(exaA)
CID: P73_2982
HNE: HNE_0129(adhA)
SAL: Sala_0379
SPHK: SKP52_17900(adh)
SPHP: LH20_16360
SGI: SGRAN_3454(adhA2)
SPHU: SPPYR_0186(qbdA)
SPHI: TS85_07850
SPKC: KC8_09425
SPHR: BSY17_3920(qbdA) BSY17_934(qbdA)
SFLA: SPHFLASMR4Y_01514(qbdA)
BLAS: BSY18_3165(adhA) BSY18_3429(qgdA)
ELI: ELI_14570
AAY: WYH_01144(qbdA_1) WYH_01921(qbdA_3) WYH_02888(qbdA_4) WYH_03122(qgdA) WYH_03187(qbdA_5)
ADO: A6F68_00780(qbdA)
ABAC: LuPra_01740(qgdA_1) LuPra_02092(qbdA_3)
 » show all
Taxonomy
Reference
1  [PMID:3521592]
  Authors
Groen BW, van Kleef MA, Duine JA
  Title
Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni.
  Journal
Biochem J 234:611-5 (1986)
Reference
2  [PMID:7626615]
  Authors
de Jong GA, Caldeira J, Sun J, Jongejan JA, de Vries S, Loehr TM, Moura I, Moura JJ, Duine JA
  Title
Characterization of the interaction between PQQ and heme c in the quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni.
  Journal
Biochemistry 34:9451-8 (1995)
Reference
3  [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
Reference
4  [PMID:10320337]
  Authors
Matsushita K, Yamashita T, Aoki N, Toyama H, Adachi O
  Title
Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory chain of Pseudomonas putida HK5.
  Journal
Biochemistry 38:6111-8 (1999)
DOI:10.1021/bi990121f
Reference
5  [PMID:12057198]
  Authors
Chen ZW, Matsushita K, Yamashita T, Fujii TA, Toyama H, Adachi O, Bellamy HD, Mathews FS
  Title
Structure at 1.9 A resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5.
  Journal
Structure 10:837-49 (2002)
DOI:10.1016/S0969-2126(02)00774-8
  Sequence
Reference
6  [PMID:11714714]
  Authors
Oubrie A, Rozeboom HJ, Kalk KH, Huizinga EG, Dijkstra BW
  Title
Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer.
  Journal
J Biol Chem 277:3727-32 (2002)
DOI:10.1074/jbc.M109403200
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.1.9.1
IUBMB Enzyme Nomenclature: 1.1.9.1
ExPASy - ENZYME nomenclature database: 1.1.9.1
BRENDA, the Enzyme Database: 1.1.9.1

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