Tomato alcohol dehydrogenase: purification and substrate specificity.

  title={Tomato alcohol dehydrogenase: purification and substrate specificity.},
  author={T. Bicsak and L. Kann and A. Reiter and T. Chase},
  journal={Archives of biochemistry and biophysics},
  volume={216 2},
Abstract Alcohol dehydrogenase of tomato ( Lycopersicon esculentum ) has been purified to homogeneity, using affinity chromatography on Cibacron F3GA-agarose. The enzyme is a dimer, M r 90,000–100,000. The coenzyme is NAD + ; no NADP + -dependent activity was detected even in crude extracts. Among saturated substrates, ethanol and acetaldehyde show the lowest apparent K m values (2.67 and 0.174 m m , respectively) and highest V values, supporting a primary role in acetaldehyde metabolism, with… 
Alcohol dehydrogenase (ADH; alcohol: NAD oxidoreductase; EC is a dimericzinc enzyme which catalyses the inter-conversion of acetaldehyde to ethanol, using NAD/NADH as a cofactor. It is the
Purification and properties of alcohol dehydrogenase from the acid- and ethanol-tolerant yeast Candida solicola
Abstract Two alcohol dehydrogenases (EC from the acid- and ethanol-tolerant yeast Candida solicola WY-1 have been purified and characterized. The microbial strain cultured in a medium
Purification and characterization of an alcohol dehydrogenase from Lithospermum erythrorhizon cell cultures
An NAD-dependent alcohol dehydrogenase has been purified to apparent homogeneity from cell suspension cultures of Lithospermum erythrorhizon Sieb. et Zucc. (Boraginaceae), using protamine sulphate
Kinetic Studies with Crude Tomato Alcohol Dehydrogenase
Tomato alcohol dehydrogenase (ADH) is very important in the formation of fresh tomato aroma volatiles. The kinetic characterization and isolation of this enzyme may promote some in vitro
Purification and characterization of a hexanol-degrading enzyme extracted from apple.
An enzyme having activity toward n-hexanol was purified from apple, and its biochemical characteristics were analyzed, which showed activity to isoamylol, 1-propanol, n- hexanol, and isobutanol but not toward methanol and ethanol.
Alcohol dehydrogenase (ADH2) from a mutant strain of Candida guilliermondii A80-03: purification and characterization.
Alcohol dehydrogenase ADH2 was purified twice from Candida guilliermondii strain A80-03, by ion exchange column chromatography on DEAE-Toyopearl 650M. The enzyme was a dimer of M(r) 98,500. ADH2 had
Concurrent synthesis and degradation of alcohol dehydrogenase in elicitor-treated and wounded potato tubers.
Results imply a turnover of ADH following elicitor treatment of potato tuber discs, as shown by nondenaturing gel electrophoresis, which involved the same ADH isozyme.
Arabidopsis formaldehyde dehydrogenase. Molecular properties of plant class III alcohol dehydrogenase provide further insights into the origins, structure and function of plant class p and liver class I alcohol dehydrogenases.
These patterns are consistent with two different metabolic roles for the ethanol-active enzymes, a more constant function, reduction of acetaldehyde during hypoxia, for class P, and a more variable function, the detoxication of alcohols and participation in metabolic conversions, forclass I.
Characterizing NAD- and NADP-dependent Alcohol Dehydrogenase Enzymes of Strawberries
The results suggest that NAD- and NADP-dependent ADH activities are integral components of flavor and fragrance volatile production in ripening strawberries.
Nucleotide sequence of an alcohol dehydrogenase gene in octoploid strawberry (Fragaria × Ananassa Duch.)
The isolation and sequence of a strawberry alcohol dehydrogenase gene from the breeding line 8343-6 is reported and nearly 100 ~ homology to a portion of a sequence needed for anaerobic induction of Adh in maize is shown.


Characterization of Plant Alcohol Dehydrogenase
There is a similarity between plant alcohol dehydrogenases and animal and yeast enzymes, i.e., Pyrazol, imidazol and pyridine inhibit plant ADH similarly to the enzyme from horse liver.
Alcohol Dehydrogenase from Thea sinensis Seeds
Alcohol dehydrogenase (alcohol: NAD oxidoreductase, E. C. 1. 1. 1. 1.) from Thea sinensis seeds (variety: Zairai) was isolated and purified about 1, 500-fold using preparative disc electrophoresis.
Purification and partial characterization of alcohol dehydrogenase from wheat.
Abstract Further support for hypotheses proposed earlier for the genetic control and subunit composition of the alcohol dehydrogenase of Triticum has been obtained through the purification and
Alcohol Dehydrogenases from Strawberry Seeds
Two alcohol dehydrogenases (alcohol: NAD oxidoreductase, EC and alcohol: NADP oxidoreductase, EC were partially purified from extracts of strawberry seeds by conventional methods.
Alcohol: NAD Oxidoreductase (E. C. from Peas
SUMMARY– The substrate specificity of the enzyme alcohol: NAD oxidoreductase from seeds and pods of the pea plant (Pisum sutivum) was investigated. The enzyme catalyzes the oxidation of primary
Aliphatic alcohol dehydrogenase from potato tubers
Abstract Potato tubers are shown to contain at least 3 alcohol dehydrogenases, one active with NAD and aliphatic alcohols, one active with NADP and terpene alcohols and one active with NADP and
L'alcool deshydrogénase de tomate (Lycopersicon esculentum): Étude cinétique et mécanisme d'action
Abstract In order to investigate the enzymatic mechanism of tomato alcohol dehydrogenase, kinetic studies were carried out at pH 5.8 and 9.4 for the forward and reverse reactions, respectively.
Purification and partial characterization of two genetically defined alcohol dehydrogenase isozymes in maize.
Amino acid analysis of the acid hydrolysates of isozymes 2F and 2S show striking similarities in the amino acid composition even though 2S is not purified to homogeneity, which suggests that these molecules differ by only one or a few amino acids.
Peanut Alcohol Dehydrogenase.
SUMMARY— Alcohol dehydrogenase (alcohol:NAD+ oxidoreductase EC has been isolated and purified from peanut kernels. The resulting preparations exhibited a high degree of purity as shown by
The mechanism of enzyme-catalyzed reduced nicotinamide adenine dinucleotide-dependent reductions. Substituent and isotope effects in the yeast alcohol dehydrogenase reaction.
  • J. Klinman
  • Chemistry, Medicine
    The Journal of biological chemistry
  • 1972
The association constants of substituted benzaldehydes for binary complex, calculated from the observed isotope effects on the limiting Michaelis constants, were found to increase with electron-donating group, and may reflect an enhanced polarization of the carbonyl of the substrate in forming the ternary complex.