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Environmental research1983; 30(2); 389-392; doi: 10.1016/0013-9351(83)90224-4

A comparative study of the effect of triazine herbicides on alcohol dehydrogenases isolated from various sources.

Abstract: The studied herbicides (terbutylazine, simazine) inhibit the activity of plant, animal, and yeast alcohol dehydrogenases. The inhibition constant Ki for alcohol dehydrogenase (ADH) isolated from peas and bakers' yeast equals approximately 10(-4) M, and that for ADH isolated from horse liver is of the order of 10(-5) M. The character of inhibition for all the herbicides studied for the reaction catalyzed by pea, liver, and yeast ADH is always noncompetitive toward ethanol and competitive with respect to NAD. The inhibition constants for the enzyme isolated from peas are pH independent. The interaction constants found for terbutylazine and simazine and for o-phenanthroline, nicotinamide, and ATP indicate that the herbicides are bonded through the metal component of the enzyme, similar to the nicotinamide part of NAD. The interaction constant less than unity found for the herbicide-ATP system indicates that the bonding site in the active center of the enzyme is different for the herbicides and the adenine part of NAD.
Publication Date: 1983-04-01 PubMed ID: 6339231DOI: 10.1016/0013-9351(83)90224-4Google Scholar: Lookup
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  • Comparative Study
  • Journal Article

Summary

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This study investigates how triazine herbicides impact the function of alcohol dehydrogenases from various sources. It finds that these herbicides inhibit the activity of these enzymes, with different inhibition rates for alcohol dehydrogenases isolated from peas, yeast, and horse liver.

Study Objective and Methodology

  • The aim of this study was to understand how triazine herbicides, specifically terbutylazine and simazine, affect the functioning of the enzyme alcohol dehydrogenase (ADH), which plays a crucial role in the metabolism of alcohol in organisms.
  • ADH was isolated from three different sources: peas (plant), bakers’ yeast (yeast), and horse liver (animal).
  • The herbicides’ inhibition constant Ki, which describes the concentration of the herbicide that reduces the enzyme’s activity to half its original value, was measured for each source of ADH.

Findings and Conclusions

  • The herbicides studied were shown to inhibit the activity of ADH from all three sources.
  • The inhibition constant Ki was roughly 10(-4) M for ADH from both peas and yeast, but measured around 10(-5) M with ADH from horse liver, suggesting a stronger inhibition effect on the latter.
  • The nature of the herbicides’ inhibition of the ADH’s catalytic reaction—turning ethanol into another compound—was found to be noncompetitive with respect to ethanol and competitive regarding NAD (Nicotinamide Adenine Dinucleotide), a crucial molecule involved in energy production in cells.
  • The apparent interaction between the herbicides and the metal component within the ADH enzyme resembles the bonding pattern of the nicotinamide part of NAD with the enzyme.
  • Findings also show that the herbicides bind to a different site within the enzyme’s active center than the adenine part of NAD, as indicated by the interaction constant of less than one for the herbicide-ATP (Adenosine Triphosphate) system. ATP is another important molecule for the storage and transfer of energy in cells.

Implications and Future Directions

  • The findings highlight the need for careful consideration in the use of such herbicides due to their potential impact on crucial metabolic processes involving ADH in organisms.
  • More research will be beneficial to confirm these findings and further investigate the specifics of the herbicides’ inhibitory mechanisms on ADH from various sources.

Cite This Article

APA
Leblová S, Galociová J, Cerovská N. (1983). A comparative study of the effect of triazine herbicides on alcohol dehydrogenases isolated from various sources. Environ Res, 30(2), 389-392. https://doi.org/10.1016/0013-9351(83)90224-4

Publication

ISSN: 0013-9351
NlmUniqueID: 0147621
Country: Netherlands
Language: English
Volume: 30
Issue: 2
Pages: 389-392

Researcher Affiliations

Leblová, S
    Galociová, J
      Cerovská, N

        MeSH Terms

        • Alcohol Oxidoreductases / antagonists & inhibitors
        • Alcohol Oxidoreductases / metabolism
        • Animals
        • Fabaceae / enzymology
        • Herbicides / pharmacology
        • Horses
        • Liver / enzymology
        • Plants, Medicinal
        • Saccharomyces cerevisiae / enzymology
        • Simazine / pharmacology
        • Triazines / pharmacology

        Citations

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