Entry |
|
Name |
alcohol dehydrogenase (azurin);
type II quinoprotein alcohol dehydrogenase;
quinohaemoprotein ethanol dehydrogenase;
QHEDH;
ADHIIB
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Class |
Oxidoreductases;
Acting on the CH-OH group of donors;
With a copper protein as acceptor
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Sysname |
alcohol:azurin oxidoreductase
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Reaction(IUBMB) |
a primary alcohol + azurin = an aldehyde + reduced azurin [RN: R09480]
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Reaction(KEGG) |
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Substrate |
primary alcohol [CPD: C00226];
azurin
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Product |
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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.
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History |
EC 1.1.9.1 created 2010 as EC 1.1.98.1; transferred 2011 to EC 1.1.9.1
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Orthology |
K17760 | quinohemoprotein ethanol dehydrogenase |
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Genes |
» show all
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Reference |
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Authors |
Groen BW, van Kleef MA, Duine JA |
Title |
Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni. |
Journal |
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Reference |
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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 |
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Reference |
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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 |
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Reference |
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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 |
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Reference |
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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 |
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Sequence |
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Reference |
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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 |
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Sequence |
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Other DBs |
ExplorEnz - The Enzyme Database: | 1.1.9.1 |
ExPASy - ENZYME nomenclature database: | 1.1.9.1 |
BRENDA, the Enzyme Database: | 1.1.9.1 |
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