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  • Title: Cations in component reactions of 'malic' enzyme catalysis.
    Author: Tsai CS, Tsai YH, Samad RA.
    Journal: Biochem J; 1971 Aug; 124(1):193-7. PubMed ID: 4399519.
    Abstract:
    The ;malic' enzyme (EC 1.1.1.40) has been purified (300-fold) from wheat germ and its abilities to catalyse the decarboxylation and the hydrogenation of oxaloacetic acid and oxaloacetate esters was studied. The free 1-carboxyl group is essential for the interaction of oxaloacetates and substituted oxaloacetates with the enzyme via cations. The free 4-carboxyl group is required for the decarboxylation but is not indispensable for the hydrogenation. At high concentrations, cations inhibit the enzymic hydrogenation of oxaloacetic acid but not that of 4-ethyl oxaloacetate. A plausible inhibitory mechanism is proposed.
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