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: 
PPW: 
PMOS: 
PSZ: 
PSR: 
PSH: 
PSTU: 
PSTT: 
PBM: 
PSK: 
PPSY: 
PBB: 
MSR: 
MARI: 
GPS: 
ZAL: 
ADI: 
B5T_04379(exaA1)
SDF: 
PSPI: 
REU: 
REH: 
H16_A1884(h16_A1884)
CNC: 
CTI: 
CBW: 
AMIM: 
MIM_c00090(qheDH1)
POL: 
VEI: 
DAC: 
DEL: 
VAP: 
VPE: 
VPD: 
CTT: 
CTES: 
MPT: 
PBH: 
AAW51_3568(qheDH)
AZO: 
azo2844(exaA1) azo3022(exaA4)
THU: 
AGE: 
PLA: 
BJU: 
BBT: 
RPA: 
RPB: 
RPD: 
RPE: 
RPT: 
RPX: 
HMC: 
PZU: 
CID: 
HNE: 
HNE_0129(adhA)
HBC: 
NAR: 
NPP: 
NPN: 
SAL: 
SPHK: 
SPHP: 
SMAG: 
STER: 
SWI: 
SPHI: 
SJP: 
SCH: 
SSY: 
SYB: 
SPHG: 
ELI: 
AAY: 
WYH_01144(qbdA_1) WYH_01921(qbdA_3) WYH_02888(qbdA_4) WYH_03122(qgdA) WYH_03187(qbdA_5)
 » 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 (1986) 611-5.
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 (1995) 9451-8.
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 (1995) 2442-50.
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 (1999) 6111-8.
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 (2002) 837-49.
  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 (2002) 3727-32.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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