Structure of glyoxysomal malate dehydrogenase (MDH3) from Saccharomyces cerevisiae.

ABSTRACT: Malate dehydrogenase (MDH), a carbohydrate and energy metabolism enzyme in eukaryotes, catalyzes the interconversion of malate to oxaloacetate (OAA) in conjunction with that of nicotinamide adenine dinucleotide (NAD⁺) to NADH. Three isozymes of MDH have been reported in Saccharomyces cerevisiae: MDH1, MDH2 and MDH3. MDH1 is a mitochondrial enzyme and a member of the tricarboxylic acid cycle, whereas MDH2 is a cytosolic enzyme that functions in the glyoxylate cycle. MDH3 is a glyoxysomal enzyme that is involved in the reoxidation of NADH, which is produced during fatty-acid β-oxidation. The affinity of MDH3 for OAA is lower than those of MDH1 and MDH2. Here, the crystal structures of yeast apo MDH3, the MDH3-NAD⁺ complex and the MDH3-NAD⁺-OAA ternary complex

SUBMITTER: Moriyama S 

PROVIDER: S-EPMC6168765 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature