|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Protein-Modification Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions → Protein-Modification Reactions|
EC Number: 188.8.131.52
Supersedes EC number: 184.108.40.206
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Mass balance status: 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
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.
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
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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