Cations in component reactions of ‘malic’ enzyme catalysis
- 1 August 1971
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 124 (1), 193-197
- https://doi.org/10.1042/bj1240193
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.Keywords
This publication has 7 references indexed in Scilit:
- Oxalacetate decarboxylase from cod. Mechanism of action and stereoselective reduction of pyruvate by borohydrideBiochemistry, 1968
- PIGEON LIVER MALIC ENZYME .2. ISOLATION CRYSTALLIZATION AND SOME PROPERTIES1967
- PIGEON LIVER MALIC ENZYME .5. KINETIC STUDIES1967
- Some properties of the malic enzyme of pigeon liver. 1. Conversion of malate into pyruvateBiochemical Journal, 1959
- Purification and Properties of Pigeon Liver Malic EnzymeJournal of Biological Chemistry, 1958
- BIOSYNTHESIS OF DICARBOXYLIC ACIDS BY CARBON DIOXIDE FIXATION .8. EQUILIBRIUM OF MALIC ENZYME REACTION1953
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951