Malate dehydrogenase (EC 1.1.1.37) (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 1.1.1.82) 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 [3]: an aspartic acid which
is involved in a proton relay mechanism, and an arginine which binds the
substrate.
MDH from archaebacteria do not belong to the above family; they are
evolutionary related to lactate dehydrogenases [4].
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