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MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical ReactionsProtein-Modification Reactions
Reactions Classified By SubstrateMacromolecule ReactionsProtein-ReactionsProtein-Modification Reactions

EC Number:

Enzymes and Genes:

Comamonas testosteroni: alcohol dehydrogenase (azurin)Inferred from experiment: qheDH

Supersedes EC number:

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Mass balance status: Balance undetermined; a substrate lacks a chemical formula

Enzyme Commission Primary Name: alcohol dehydrogenase (azurin)

Enzyme Commission Synonyms: type II quinoprotein alcohol dehydrogenase, quinohaemoprotein ethanol dehydrogenase, QHEDH, ADHIIB

Taxonomic Range: Bacteria

Enzyme Commission Summary:
A soluble, periplasmic PQQ-containing quinohaemoprotein. Also contains a single haem c. Occurs in Comamonas and Pseudomonas. Does not require an amine activator. Oxidises 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 methosulphate 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 disulphide ring structure in close proximity to the PQQ.

Citations: [Groen86, deJong95, Toyama95, Matsushita99, Chen02, Oubrie02]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:

Created 17-Mar-2010 by Caspi R, SRI International


Chen02: Chen ZW, Matsushita K, Yamashita T, Fujii TA, Toyama H, Adachi O, Bellamy HD, Mathews FS (2002). "Structure at 1.9 A resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5." Structure 10(6);837-49. PMID: 12057198

deJong95: de Jong GA, Caldeira J, Sun J, Jongejan JA, de Vries S, Loehr TM, Moura I, Moura JJ, Duine JA (1995). "Characterization of the interaction between PQQ and heme c in the quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni." Biochemistry 34(29);9451-8. PMID: 7626615

Groen86: Groen BW, van Kleef MA, Duine JA (1986). "Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni." Biochem J 234(3);611-5. PMID: 3521592

Matsushita99: Matsushita K, Yamashita T, Aoki N, Toyama H, Adachi O (1999). "Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory chain of Pseudomonas putida HK5." Biochemistry 38(19);6111-8. PMID: 10320337

Oubrie02: Oubrie A, Rozeboom HJ, Kalk KH, Huizinga EG, Dijkstra BW (2002). "Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer." J Biol Chem 277(5);3727-32. PMID: 11714714

Toyama95: Toyama H, Fujii A, Matsushita K, Shinagawa E, Ameyama M, Adachi O (1995). "Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols." J Bacteriol 177(9);2442-50. PMID: 7730276

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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