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PH Effects on Cytoplasmic Aldehyde Dehydrogenase from Sheep Liver

  • Paul D. Buckley
  • Rosemary L. Motion
  • Leonard F. Blackwell
  • Jeremy P. Hill
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 284)

Abstract

Although studies on the effect of pH on aldehyde dehydrogenase have been carried out in a number of laboratories, the results of these studies do not give a complete picture of the mechanism of the aldehyde dehydrogenase catalyzed oxidation of propionaldehyde over an extended pH range. The enzyme catalyzed oxidation reaction at pH 7.0 and 7.6 is generally agreed to occur by the following ordered mechanism:
$$E \rightleftharpoons E.NA{D^ + } \rightleftharpoons E.NA{D^ + }.ALD \rightleftharpoons E.NADH.acyl \to *E.NADH \rightleftharpoons E.NADH \rightleftharpoons E$$
Scheme I At least at low propionaldehyde concentrations, the rate of the reaction is controlled by the slow conformational change which occurs during the release of NADH from the enzyme (Blackwell et al., 1987; Dickinson, 1985).

Keywords

Aldehyde Dehydrogenase Propionaldehyde Oxidation Constant Ionic Strength Displacement Rate Constant Sheep Liver 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Paul D. Buckley
    • 1
  • Rosemary L. Motion
    • 2
  • Leonard F. Blackwell
    • 1
  • Jeremy P. Hill
    • 1
  1. 1.Department of Chemistry and BiochemistryMassey UniversityPalmerston NorthNew Zealand
  2. 2.New Zealand Dairy Research InstitutePalmerston NorthNew Zealand

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