L-Alloisocitrate dehydrogenase and oxalosuccinate decarboxylase from a Pseudomonas sp. utilizing L-alloisocitrate.
Two novel enzymes, NAD+-linked L-alloisocitrate (erythro-Ls-isocitrate) dehydrogenase and oxalosuccinate decarboxylase, were found and purified from a strain of Pseudomonas isolated as an L-alloisocitrate utilizing bacterium. The former enzyme catalyzes a reversible oxidation-reduction between L-alloisocitrate and oxalosuccinate which favors oxalosuccinate reduction. The latter enzyme catalyzes rapid decarboxylation of oxalosuccinate to alpha-ketoglutarate and CO2. Both enzymes require no metals for their activities. Complete oxidative decarboxylation of L-alloisocitrate to alpha-ketoglutarate occurs as a result of the sequential reactions catalyzed by these two enzymes. L-Alloisocitrate induces both enzymes in the growing pseudomonad.
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D004355:Drug Stability; D007521:Isocitrate Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*; D007523:Isocitrates / Q000378:metabolism*; D007700:Kinetics; D009243:NAD; D010070:Oxalates / Q000302:isolation & purification / Q000378:metabolism; D011549:Pseudomonas / Q000201:enzymology*; D013386:Succinates / Q000302:isolation & purification / Q000378:metabolism
D007523:Isocitrates; D010070:Oxalates; D013386:Succinates; D009243:NAD; D000429:Alcohol Oxidoreductases; C026047:alloisocitrate dehydrogenase; D007521:Isocitrate Dehydrogenase; C039355:isocitrate dehydrogenase (NADP+)