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

\rightleftharpoons

aldehyde + reduced azurin

This enzyme is a periplasmic PQQ-containing quinohemoprotein.

References

↑ Groen, B.W.; van Kleef, M.A.; 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.; 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.; 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.; 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.; 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.; 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.

External links

Alcohol dehydrogenase (azurin) at the US National Library of Medicine Medical Subject Headings (MeSH)

Oxidoreductases: alcohol oxidoreductases (EC 1.1)

1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase Alcohol dehydrogenase Aldo-keto reductase 1A1 1B1 1B10 1C1 1C3 1C4 7A2 Aldose reductase Beta-Ketoacyl ACP reductase Carbohydrate dehydrogenases Carnitine dehydrogenase D-malate dehydrogenase (decarboxylating) DXP reductoisomerase Glucose-6-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase HMG-CoA reductase IMP dehydrogenase Isocitrate dehydrogenase Lactate dehydrogenase L-threonine dehydrogenase L-xylulose reductase Malate dehydrogenase Malate dehydrogenase (decarboxylating) Malate dehydrogenase (NADP+) Malate dehydrogenase (oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) Phosphogluconate dehydrogenase Sorbitol dehydrogenase Hydroxysteroid dehydrogenase: 3 Beta 3-beta-HSD NSDHL 11 Beta HSD11B1 HSD11B2 17 Beta

1.1.2: cytochrome acceptor	D-lactate dehydrogenase (cytochrome) D-lactate dehydrogenase (cytochrome c-553) Mannitol dehydrogenase (cytochrome)

1.1.3: oxygen acceptor	Glucose oxidase L-gulonolactone oxidase Xanthine oxidase

1.1.4: disulfide as acceptor	Vitamin K epoxide reductase Vitamin-K-epoxide reductase (warfarin-insensitive)

1.1.5: quinone/similar acceptor	Malate dehydrogenase (quinone) Quinoprotein glucose dehydrogenase

1.1.99: other acceptors	Choline dehydrogenase L2HGDH

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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