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Biochimica et biophysica acta1975; 384(1); 1-11; doi: 10.1016/0005-2744(75)90090-x

An examination of octanol and octanal metabolism to octanoic acid by horse liver alcohol dehydrogenase.

Abstract: The kinetics of the horse liver alcohol dehydrogenase (alcohol: NAD+ oxidoreductase EC 1.1.1.1) catalyzed metabolism of octanol and octanal to octanoic acid have been examined. On incubation of octanol with horse liver alcohol dehydrogenase in the presence of NAD+, NADH as well as octanal and octanoic acid were seen as the initial products. However, on continued incubation, the octanal concentration progressively decreased to where only negligible quantities were present in the incubation after 10 min. The production of NADH was biphasic. An initial phase was followed in about 2 min with a slower but linear rate of NADH production. The production of octanoic acid was approximately linear throughout the 10 min incubation period. Since octanal is an intermediate in the oxidation of octanol to octanoic acid, the ability of semicarbazide to inhibit the metabolism of octanol to octanoic acid was examined. At a concentration of semicarbazide which was 63 times the concentration of octanol in the incubation media, the rate of formation of octanoic acid was inhibited by only 30%. The results of these experiments suggest that in the oxidation of octanol to octanoic acid a portion of the octanal formed from octanol is not released from the enzyme but, in the presence of NAD+, is oxidized to octanoic acid.
Publication Date: 1975-03-28 PubMed ID: 165828DOI: 10.1016/0005-2744(75)90090-xGoogle Scholar: Lookup
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  • Journal Article
  • Research Support
  • U.S. Gov't
  • P.H.S.

Summary

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The research article presents an investigation into how horse liver alcohol dehydrogenase catalyzes the metabolism of octanol and octanal into octanoic acid with the use of NAD+ and observation of NADH production. The process is analysed in time phases, and the effect of a semicarbazide inhibitor on the process is also examined.

Objective and Methodology

  • The research aimed to understand the kinetics of how horse liver alcohol dehydrogenase (a type of enzyme) is responsible for converting octanol and octanal into octanoic acid.
  • The study involved incubating octanol with horse liver alcohol dehydrogenase in the presence of NAD+, an essential molecule involved in oxidation-reduction reactions in metabolism, and monitoring the production of NADH (a reduced form of NAD+), octanal, and octanoic acid over time.
  • The experiment was also repeated with the introduction of semicarbazide to test its inhibitory effects on the metabolic process.

Initial Observations

  • Following the incubation process, octanal and octanoic acid were initially produced alongside NADH.
  • The researchers noticed that the octanal concentration started to decrease after a certain period of time, and was almost negligible after 10 minutes of incubation.

NADH and Octanoic Acid Production

  • The production of NADH was observed in two phases. The first phase experienced a rapid production of NADH, followed by a slower, linear rate of manufacturing in about 2 minutes.
  • Octanoic acid production progressed approximately at a linear rate throughout the 10-minute incubation period.

Impact of Semicarbazide and Conclusions

  • Considering octanal as an intermediate product in the oxidation of octanol to octanoic acid, the inhibitory impact of semicarbazide on this metabolic process was examined.
  • It was found that even 63 times higher concentration of semicarbazide than octanol only reduced the formation rate of octanoic acid by 30%.
  • The results suggest that some quantity of octanal produced from octanol is not released from the enzyme but is instead further oxidized to octanoic acid in the presence of NAD+.

Cite This Article

APA
Hinson JA, Neal RA. (1975). An examination of octanol and octanal metabolism to octanoic acid by horse liver alcohol dehydrogenase. Biochim Biophys Acta, 384(1), 1-11. https://doi.org/10.1016/0005-2744(75)90090-x

Publication

ISSN: 0006-3002
NlmUniqueID: 0217513
Country: Netherlands
Language: English
Volume: 384
Issue: 1
Pages: 1-11

Researcher Affiliations

Hinson, J A
    Neal, R A

      MeSH Terms

      • Alcohol Oxidoreductases / metabolism
      • Alcohols / metabolism
      • Aldehydes / metabolism
      • Animals
      • Caprylates / metabolism
      • Horses
      • Kinetics
      • Liver / enzymology
      • NAD
      • Octanols / metabolism
      • Semicarbazides / pharmacology
      • Time Factors

      Citations

      This article has been cited 1 times.
      1. Nahab FB, Wittevrongel L, Ippolito D, Toro C, Grimes GJ, Starling J, Potti G, Haubenberger D, Bowen D, Buchwald P, Dong C, Kalowitz D, Hallett M. An open-label, single-dose, crossover study of the pharmacokinetics and metabolism of two oral formulations of 1-octanol in patients with essential tremor. Neurotherapeutics 2011 Oct;8(4):753-62.
        doi: 10.1007/s13311-011-0045-1pubmed: 21594724google scholar: lookup