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Alcohol dehydrogenase (azurin)
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EC no.1.1.9.1
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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[edit]

  1. ^ Groen BW, van Kleef MA, Duine JA (March 1986). "Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni". The Biochemical Journal. 234 (3): 611–5. doi:10.1042/bj2340611. PMC 1146615. PMID 3521592.
  2. ^ de Jong GA, Caldeira J, Sun J, Jongejan JA, de Vries S, Loehr TM, Moura I, Moura JJ, Duine JA (July 1995). "Characterization of the interaction between PQQ and heme c in the quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni". Biochemistry. 34 (29): 9451–8. doi:10.1021/bi00029a021. PMID 7626615.
  3. ^ Toyama H, Fujii A, Matsushita K, Shinagawa E, Ameyama M, Adachi O (May 1995). "Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols". Journal of Bacteriology. 177 (9): 2442–50. doi:10.1128/jb.177.9.2442-2450.1995. PMC 176903. PMID 7730276.
  4. ^ Matsushita K, Yamashita T, Aoki N, Toyama H, Adachi O (May 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. doi:10.1021/bi990121f. PMID 10320337.
  5. ^ Chen ZW, Matsushita K, Yamashita T, Fujii TA, Toyama H, Adachi O, Bellamy HD, Mathews FS (June 2002). "Structure at 1.9 A resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5". Structure. 10 (6): 837–49. doi:10.1016/s0969-2126(02)00774-8. PMID 12057198.
  6. ^ Oubrie A, Rozeboom HJ, Kalk KH, Huizinga EG, Dijkstra BW (February 2002). "Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer". The Journal of Biological Chemistry. 277 (5): 3727–32. doi:10.1074/jbc.M109403200. PMID 11714714.

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