EC 1.1.9.1 - Alcohol dehydrogenase (azurin)

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IntEnz Enzyme Nomenclature
EC 1.1.9.1

Names

Accepted name:
alcohol dehydrogenase (azurin)
Other names:
type II quinoprotein alcohol dehydrogenase
quinohemoprotein ethanol dehydrogenase
QHEDH
ADHIIB
Systematic name:
alcohol:azurin oxidoreductase

Reaction

Cofactors

Comments:

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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Groen, B. W., van Kleef, M. A., Duine, J. A.
    Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni.
    Biochem. J. 234: 611-615 (1986). [PMID: 3521592]
  2. de Jong, G. A., Caldeira, J., Sun, J., Jongejan, J. A., de Vries, S., Loehr, T. M., Moura, I., Moura, J. J., Duine, J. A.
    Characterization of the interaction between PQQ and heme c in the quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni.
    Biochemistry 34: 9451-9458 (1995). [PMID: 7626615]
  3. Toyama, H., Fujii, A., Matsushita, K., Shinagawa, E., Ameyama, M., Adachi, O.
    Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols.
    J. Bacteriol. 177: 2442-2450 (1995). [PMID: 7730276]
  4. Matsushita, K., Yamashita, T., Aoki, N., Toyama, H., Adachi, O.
    Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory chain of Pseudomonas putida HK5.
    Biochemistry 38: 6111-6118 (1999). [PMID: 10320337]
  5. Chen, Z. W., Matsushita, K., Yamashita, T., Fujii, T. A., Toyama, H., Adachi, O., Bellamy, H. D., Mathews, F. S.
    Structure at 1.9 Å resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5.
    Structure 10: 837-849 (2002). [PMID: 12057198]
  6. Oubrie, A., Rozeboom, H. J., Kalk, K. H., Huizinga, E. G., Dijkstra, B. W.
    Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer.
    J. Biol. Chem. 277: 3727-3732 (2002). [PMID: 11714714]

[EC 1.1.9.1 created 2010 as EC 1.1.98.1; transferred 2011 to EC 1.1.9.1]