Isolation and properties of a 'malic' enzyme from cauliflower bud mitochondria.
1. A ;malic' enzyme [l-malate-NAD oxidoreductase (decarboxylating), EC 1.1.1.39] has been isolated from cauliflower bud mitochondria and partially purified. 2. The enzyme is specific for l-malate and has an absolute requirement for either Mn(2+), Co(2+) or Mg(2+). 3. The enzyme shows activity with both NAD(+) and NADP(+), but NAD(+) is the preferred cofactor. 4. No appreciable oxaloacetate decarboxylase activity is present in the enzyme preparations even at low pH values. 5. The enzyme is inhibited by NADH and by oxaloacetate and stimulated by SO(4) (2-) and by low concentrations of CoA. 6. The regulatory properties of the enzyme support the proposed role of the enzyme in the utilization of tricarboxylic acid-cycle acids for energy production when glycolysis is suppressed.
D003035:Cobalt; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D008274:Magnesium; D008291:Malate Dehydrogenase / Q000302:isolation & purification*; D008345:Manganese; D008928:Mitochondria / Q000201:enzymology*; D009243:NAD; D009249:NADP; D010940:Plant Proteins / Q000032:analysis; D010944:Plants / Q000201:enzymology*; D013053:Spectrophotometry; D014675:Vegetables
D010940:Plant Proteins; D009243:NAD; D003035:Cobalt; D008345:Manganese; D009249:NADP; D008291:Malate Dehydrogenase; D008274:Magnesium