|PROSITE documentation PDOC00066|
Malate dehydrogenase (EC 126.96.36.199) (MDH) [1,2] catalyzes the interconversion of malate to oxaloacetate utilizing the NAD/NADH cofactor system. The enzyme participates in the citric acid cycle and exists in all aerobics organisms.
While prokaryotic organisms contains a single form of MDH, in eukaryotic cells there are two isozymes: one which is located in the mitochondrial matrix and the other in the cytoplasm. Fungi and plants also harbor a glyoxysomal form which functions in the glyoxylate pathway. In plants chloroplast there is an additional NADP-dependent form of MDH (EC 188.8.131.52) which is essential for both the universal C3 photosynthesis (Calvin) cycle and the more specialized C4 cycle.
As a signature pattern for this enzyme we have chosen a region that includes two residues involved in the catalytic mechanism : an aspartic acid which is involved in a proton relay mechanism, and an arginine which binds the substrate.Note:
MDH from archaebacteria do not belong to the above family; they are evolutionary related to lactate dehydrogenases .Last update:
November 1995 / Text revised.
PROSITE method (with tools and information) covered by this documentation:
|Source||Trends Biochem. Sci. 13:178-181(1988).|
|Title||Malate dehydrogenase isoenzymes: cellular locations and role in the flow of metabolites between the cytoplasm and cell organelles.|
|Source||Biochim. Biophys. Acta 1100:217-234(1992).|
|3||Authors||Birktoft J.J., Rhodes G., Banaszak L.J.|
|Title||Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-A resolution.|
|4||Authors||Cendrin F., Chroboczek J., Zaccai G., Eisenberg H., Mevarech M.|
|Title||Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui.|