Addition products of diphosphopyridine nucleotides with substrates of pyridine nucleotide-linked dehydrogenases

Everse, Johannes; Zoll, Estelle C.; Kahan, Lawrence; Kaplan, Nathan O.

doi:10.1016/0045-2068(71)90017-4

Cited by 93 publications

(42 citation statements)

References 38 publications

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“…We suggest a mechanism more consistent with the available evidence is a synchronous elimination of the hydride ion and hydroxyl proton, perhaps involving base catalysis by a suitable group in the active site as suggested for lactate dehydrogenase [30]. The participation of a histidine residue acting as a base has been postulated [31] on the basis of the pHdependence of the pre-steady-state rate constant for ethanol.…”

Section: Nature Of the Hydrogen-transfersupporting

confidence: 50%

Substituent Effects on the Pre‐Steady‐State Kinetics of Oxidation of Benzyl Alcohols by Liver Alcohol Dehydrogenase

Hardman

Blackwell

Boswell

et al. 1974

European Journal of Biochemistry

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1. The oxidation of benzyl alcohols by liver alcohol dehydrogenase under conditions [S], $-[El, is a biphasic process with exponential rise to a steady state. The rate constants for the transient phase were determined by a curve-fitting procedure.2. A large isotope effect was obtained for p-methoxybenzyl alcohol, indicating that hydrogen transfer is rate-determining for the transient phase. Rate constants for the hydrogen transfer step, k3, were obtained for the various alcohols and correlated with the Hammett o constant by plotting log k3 against o. The slope of this line (e = -0.76) is consistent with rate-limiting hydride transfer; a mechanism is proposed to account for the low magnitude of e. 3.The pre-steady-state rate constants, kb, for all benzyl alcohols (c 20 s-') are lower than that for ethanol. 2-Methylpropan-1-01 and cyclohexylmethanol have pre-steady-state rate constants of about 150 s-', indicating that the lower kh values for benzyl alcohols are due to the electronwithdrawing effect of the benzene ring, rather than to steric effects.Steady-state and transient kinetic studies on liver alcohol dehydrogenase have established that the reaction proceeds by an ordered mechanism with coenzyme binding first, and coenzyme dissocation as the rate-determining step at saturating concentrations [I -41. The existence of ternary complexes in the reaction mechanism was indicated by product inhibition studies [4,5]. Subsequently Shore and Gutfreund [6] studied the pre-steady-state formation of NADH during the oxidation of ethanol by alcohol dehydrogenase in order to measure the rate of interconversion of the ternary complexes. They found a substantial kinetic isotope effect on the rate constant for initial formation of enzyme-bound NADH, indicating that the hydrogen transfer step was ratelimiting for the transient phase [6].Substrate structure has been found to have a marked effect on the rate of the hydrogen transfer step [7]. A pre-steady-state burst of bound NADH was observed [7] during the oxidation of two primary alcohols, ethanol and I-propanol ; however no burst was observed for methanol or the secondary alcohol, 2-propanol, because for these alcohols the hydrogen transfer step was slower than NADH dissociation and hence rate-determining for the steady-state phase.~.

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Section: Nature Of the Hydrogen-transfersupporting

confidence: 50%

Substituent Effects on the Pre‐Steady‐State Kinetics of Oxidation of Benzyl Alcohols by Liver Alcohol Dehydrogenase

Hardman

Blackwell

Boswell

et al. 1974

European Journal of Biochemistry

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“…In cases in which the interaction between the bifunctional ligand and the enzyme is not sufficiently strong, formation of ternary complexes could be tried as exemplified here. Thus, besides dead-end complex formation also other ternary complexes could be utilized, for instance complexes with coenzyme and inhibitor and complexes with coenzyme-substrate adducts [9]. Alternatively, a careful addition of salts, e.g., ammonium sulphate or solvents, e.g., polyethylene glycol might enhance the precipitation without impairing the specificity.…”

Section: Resultsmentioning

confidence: 99%

Affinity precipitation of enzymes

Larsson

Mosbach

1979

FEBS Letters

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“…In each homozygous strain of B. oleae three molecular forms of the enzyme are present. Schwartz et al (1975) and Schwartz and Sofer (1976) have confirmed that, in Drosophila melanogaster, these additional forms of the enzyme originate from the tight, but non-covalent, binding of one or two molecules of a NAD-carbonyl addition compound (Everse et al, 1971) to the native enzyme. Schwartz and Sofer (1976) found that exposing D. melanogaster flies to a variety of carbonyl compounds, whose structures were similar to substrates of ADH, resulted in an increase in activity of those forms postulated to carry a NAD-carbonyl compound and a decrease in activity in the major form of the enzyme, thought to be free of the compound.…”

Section: Introductionmentioning

confidence: 56%

Effect of acetone feeding on alcohol dehydrogenase activity in the olive fruit fly, Bactrocera oleae

et al. 2002

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The purpose of this study is to demonstrate a clear connection between the presence of acetone in larval diet and alcohol dehydrogenase (ADH) activity in laboratory raised populations of Bactrocera oleae. ADH activity of B. oleae is depressed in acetone-impregnated diets. At the same time the change of activity is accompanied by a change in the relative proportions of the multiple forms of ADH. The bulk of activity in the most cathodally migrating form is lost, and all the activity becomes localized in the less cathodally migrating forms of the enzyme. Moreover, ADH activity, expressed in vivo, appears to drop after exposure to ace-

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Addition products of diphosphopyridine nucleotides with substrates of pyridine nucleotide-linked dehydrogenases

Cited by 93 publications

References 38 publications

Substituent Effects on the Pre‐Steady‐State Kinetics of Oxidation of Benzyl Alcohols by Liver Alcohol Dehydrogenase

Substituent Effects on the Pre‐Steady‐State Kinetics of Oxidation of Benzyl Alcohols by Liver Alcohol Dehydrogenase

Affinity precipitation of enzymes

Effect of acetone feeding on alcohol dehydrogenase activity in the olive fruit fly, Bactrocera oleae

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