Aliphatic alcohol dehydrogenase from potato tubers

Davies, Daniel; Patil, K. D.; Ugochukwu, Emmanuel N.; Towers, G.H.N.

doi:10.1016/s0031-9422(00)84438-6

Cited by 34 publications

(7 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…n.c., dehydrogenase from young stems of Forsythia suspensa [17]. Only one other aromatic alcohol dehydrogenase has been reported from higher plants [18]. This enzyme from potato tubers possessed broad aromatic substrate specificities.…”

Section: Discussionmentioning

confidence: 99%

Purification and Properties of Isoenzymes of Cinnamyl-Alcohol Dehydrogenase from Soybean-Cell-Suspension Cultures

1975

View full text Add to dashboard Cite

Two isoenzymes of an NADP' -dependent cinnamyl alcohol dehydrogenase and an NAD + -dependent aliphatic alcohol dehydrogenase were extracted from cell suspension cultures of soybean (Glycine max L., var. Mandarin) which form lignin during growth. These enzymes could be separated from each other by chromatography on DEAE-cellulose and hydroxyapatite. The cinnamyl alcohol dehydrogenase isoenzymes were partially purified by (NH&SO, fractionation, and column chromatography on DEAE-cellulose, SephadexG-100, and hydroxyapatite. The molecular weight of the enzymes were estimated by the elution volumes from a Sephadex G-100 column and were found to be about 43000 (isoenzyme 1) and 69000 (isoenzyme 2). Maximum rates of reaction were observed in the case of coniferyl alcohol oxidation at pH 9.2 (isoenzyme 1) and pH 8.8 (isoenzyme 2); in the reverse reaction pH 6.5 was optimal for isoenzyme 2.Whereas isoenzyme 1 is specific for coniferyl alcohol, isoenzyme 2 can also oxidize cinnamyl alcohol and a number of substituted cinnamyl alcohols. K , values for substituted cinnamaldehydes are 3 -11 times lower than for the corresponding alcohols. Neither isoenzyme reacted with benzyl alcohol, anisic alcohol or ethanol. Substrate inhibition for the forward and reverse reaction was found with isoenzyme 2 but not with isoenzyme 1. The equilibrium constant was determined to be about lo9 in favour of coniferaldehyde reduction. The possible role of the cinnamyl alcohol dehydrogenase in lignin biosynthesis is discussed.We have previously shown that an enzyme preparation from cell suspension cultures of soybean (Glycine max) catalyses the NADPH-dependent reduction We now describe the partial purification of two specific cinnamyl alcohol dehydrogenase isoenzymes from soybean cell suspension cultures. MATERIALS AND METHODS MatrriulsSubstituted cinnamic acids and coniferyl alcohol were purchased from C. Roth (Karlsruhe). Lithium aluminium-tris (tert-butyloxyhydride) was obtained from Fluka AG (Buchs, SG, Switzerland). All biochemicals were purchased from Boehringer Mannheim GmbH (Mannheim) or Serva (Heidelberg).Svnthesis of Substituted Cinnamyl Alcohols and Cinnamaldehydes p-Coumaryl alcohol [7] and sinapyl alcohol [8] were synthesized according to published methods. In analogy to these methods, 3,4-dimethoxycinnamyI alcohol (A, , , = 267 nm) was obtained from methyl 3,4-dimethoxycinnamate by reduction with LiAIH,. p-Coumaryl, coniferyl and sinapyl alcohol were purified by paper chromatography on Whatman 3 MM (prewashed with 10mM EDTA, 10% acetic acid, methanol, water) with the solvent system of butanol (water-saturated) containing 2 7,; NH3 [9]. For the purification of 3,4-dimethoxycinnamyl alcohol, 2 %, acetic acid was used as solvent system.

show abstract

Section: Discussionmentioning

confidence: 99%

Purification and Properties of Isoenzymes of Cinnamyl-Alcohol Dehydrogenase from Soybean-Cell-Suspension Cultures

1975

View full text Add to dashboard Cite

show abstract

“…This may best be illustrated by: n-hexan-l-ol-n-hexanal and n-hex-írans-2-en-l-ol-n-hexirans-2-enal, where the presence of the 2-double bond increased the K value 100-fold from 1.4 x 10-11 to 1.4 X 10" 9 M at pH 8 (Eriksson, 1968). Recent studies on the substrate specificity of dehydrogenase from oranges (Bruemmer and Roe, 1971) and potato (Davies et al, 1973) basically arrived at the same result.…”

Section: Alcohol Dehydrogenasementioning

confidence: 99%

Aroma compounds derived from oxidized lipids. Biochemical and analytical aspects

Eriksson¹

1975

J. Agric. Food Chem.

View full text Add to dashboard Cite

“…The maximal rate of conversion was observed when both NAD and NADP were included in the reaction mixture. Alcohol dehydrogenases of potato which catalyze oxidation of aliphatic alcohols, terpene alcohols, and aromatic alcohols have specificity for NAD, NADP, and NADP, respectively (5,6). NADP is the preferred cofactor for the conversion of cw-hydroxyfatty acid to dicarboxylic acid, catalyzed by the enzyme preparation from epidermis of V. faba (13).…”

Section: Resultsmentioning

confidence: 99%

“…Since alcohol dehydrogenase of potato does catalyze the oxidation of alcohols which are significantly larger than ethanol, even though only at very slow rates (5), it might also catalyze the oxidation of w-hydroxyacid. It was important to ascertain whether alcohol dehydrogenase and whydroxyacid dehydrogenase are two separate enzymes.…”

Section: Resultsmentioning

confidence: 99%