Alcohol dehydrogenase (azurin)
Alcohol dehydrogenase (azurin) (EC 1.1.9.1, type II quinoprotein alcohol dehydrogenase, quinohaemoprotein ethanol dehydrogenase, QHEDH, ADHIIB) is an enzyme with systematic name alcohol:azurin oxidoreductase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
- primary alcohol + azurin
aldehyde + reduced azurin
This enzyme is a periplasmic PQQ-containing quinohemoprotein.
References
- ↑ Groen, B.W., van Kleef, M.A. and Duine, J.A. (1986). "Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni". Biochem. J. 234 (3): 611–615. PMC 1146615. PMID 3521592.
- ↑ de Jong, G.A., Caldeira, J., Sun, J., Jongejan, J.A., de Vries, S., Loehr, T.M., Moura, I., Moura, J.J. and Duine, J.A. (1995). "Characterization of the interaction between PQQ and heme c in the quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni". Biochemistry 34 (29): 9451–9458. doi:10.1021/bi00029a021. PMID 7626615.
- ↑ Toyama, H., Fujii, A., Matsushita, K., Shinagawa, E., Ameyama, M. and Adachi, O. (1995). "Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols". J. Bacteriol. 177 (9): 2442–2450. PMC 176903. PMID 7730276.
- ↑ Matsushita, K., Yamashita, T., Aoki, N., Toyama, H. and 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): 6111–6118. doi:10.1021/bi990121f. PMID 10320337.
- ↑ Chen, Z.W., Matsushita, K., Yamashita, T., Fujii, T.A., Toyama, H., Adachi, O., Bellamy, H.D. and Mathews, F.S. (2002). "Structure at 1.9 Å resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5". Structure 10 (6): 837–849. doi:10.1016/s0969-2126(02)00774-8. PMID 12057198.
- ↑ Oubrie, A., Rozeboom, H.J., Kalk, K.H., Huizinga, E.G. and Dijkstra, B.W. (2002). "Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer". J. Biol. Chem. 277 (5): 3727–3732. doi:10.1074/jbc.M109403200. PMID 11714714.
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