Tomato alcohol dehydrogenase: purification and substrate specificity.

@article{Bicsak1982TomatoAD,
  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},
  year={1982},
  volume={216 2},
  pages={
          605-15
        }
}
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: A MOLECULAR MARKER IN GRAPEVINE
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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
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TLDR
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.
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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
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TLDR
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.
TLDR
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
TLDR
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.)
TLDR
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.
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TLDR
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.
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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.
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TLDR
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  • J. Klinman
  • Chemistry, Medicine
    The Journal of biological chemistry
  • 1972
TLDR
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.
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