Evidence for two immunologically distinct acetyl-CO-enzyme a synthetases in yeast

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Abstract

  • 1.

    1. In this investigation, some immunological properties of the yeast acetyl-CoA synthetase [acetate: CoA ligase (AMP), EC 6.2.1.1] elaborated under aerobic and non-aerobic conditions are presented.

  • 2.

    2. The antibody produced by each enzyme is immunologically specific. No evidence was found for the presence of inhibitory agent(s) in either enzyme extract which inhibited the heterologous enzyme antibody reaction.

  • 3.

    3. The enzyme purified from aerobic yeast was inhibited 85% by its homologous antiserum which inhibited activity of the enzyme from non-aerobic yeast by only 20%, while enzyme activity from non-aerobic yeast was inhibited 65% by its homologous antiserum, which inhibited activity from aerobic yeast by about 13%.

  • 4.

    4. Data presented in this paper indicate the presence of two distinct acetyl-CoA synthetases in this strain of yeast.

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  • Microbial acetyl-CoA metabolism and metabolic engineering

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    Citation Excerpt :

    In the second step, ACS binds CoA and converts the intermediate to acetyl-CoA and AMP. Two ACS isoforms were first identified as an ‘aerobic’ form and an ‘anaerobic’ form, which differed from each other in a number of ways, e.g. expression in certain culture conditions, enzymatic properties, cellular localizations, immunological properties and inhibition by long chain acyl-CoA (Satyanarayana and Klein, 1973, 1976; Satyanarayana et al., 1974). The ‘aerobic’ acetyl-CoA synthetase was identified to be encoded by ACS1 (Devirgilio et al., 1992).

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