A New Dye-Linked Alcohol Dehydrogenase (Vanillyl Alcohol Dehydrogenase) from Rhodopseudomonas acidophila M402 Purification, Identification of Reaction Product and Substrate Specificity

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概要

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• A new dye-linked alcohol dehydrogenase (vanillyl alcohol dehydrogenase) was purified to homogeneity from cells of Rhodopseudomonas acidophila strain M402 grown aerobically on vanillyl alcohol. The reaction product from vanillyl alcohol was identified as vanillin as judged by its melting point, elemental analysis and IR, mass and NMR spectra. The molecular weight of the enzyme was estimated to be approximately 72, 000 as determined by gel filtration and the isoelectric point was pH 6.01. The most characteristic feature of this enzyme is its wide substrate specificity range. The enzyme catalyzes the dehydrogenation of various aromatic and aliphatic alcohols and aldehydes with phenazine methosulfate as electron acceptor. The active substrates of this enzyme are as follows: Vanillyl alcohol, benzyl alcohol, cinnamyl alcohol, 2-phenylethanol, 2-phenoxyethanol, aliphatic alcohols of C2 to G8, trans-cinnamaldehyde, formaldehyde, propionaldehyde and butyraldehyde. The highest activities were obtained with vanillyl alcohol, n-propanol and n-butanol at the same level. The apparent Km values were as follows: 112μm for vanillyl alcohol, 7μm for benzyl alcohol, 180μm for n-propanol, 14μm for n-butanol, 20μm for 2-phenoxyethanol, 12μM for 2-phenylethanol and 105μm for butyraldehyde. These activities were confirmed to be catalyzed by a single enzyme by activity staining on polyacrylamide gels. But the enzyme is completely inert on vanillin and methanol. Therefore, dye-linked alcohol dehydrogenase is the most suitable name for this enzyme from R. acidophila M402 rather than vanillyl alcohol dehydrogenase or aromatic alcohol dehydrogenase, but this enzyme is substantially different from the dye-linked alcohol dehydrogenase from R. acidophila 10050 which is active on methanol.

著者

• Yamanaka Kei

  Institute Of Applied Biochemistry The University Of Tsukuba:(present Office)department Of Applied Ch

• TSUYUKI Yasutaka

  Institute of Applied Biochemistry, and Graduate School of Environmental Sciences, The University of Tsukuba

• YAMANAKA Kei

  Institute of Applied Biochemistry, and Graduate School of Masters Program in Environmental Sciences, The University of Tsukuba

関連論文

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• Identification and Characterization of a Nicotinamide Adenine Dinucleotide-Dependent p-Hydroxybenzyl Alcohol Dehydrogenase from Rhodopseudomonasacidophila M402
• Comparison of TwoDye-linked Alcohol Dehydrogenases of Rhodopseudomonas acidophila: Their Substrate Specificity and Behavior toward Oxygen
• A New Dye-Linked Alcohol Dehydrogenase (Vanillyl Alcohol Dehydrogenase) from Rhodopseudomonas acidophila M402 Purification, Identification of Reaction Product and Substrate Specificity
• Multiple Forms of Inductive and Constitutive Acyl-CoA Synthetases in Rhodopseudomonas palustris No. 82
• Isolation and Characterization of a Methanol-utilizing Phototrophic Bacterium, Rhodopseudomonas acidophila M402 and Its Growth on Vanillin Derivatives
• Butyrate Activation in Rhodopseudomonas palustris No. 82
• Occurrence of Dehydrogenases for the Metabolism of Vanillyl Alcohol in Rhodopseudomonas acidophila M402

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