Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP )

The NADP -dependent malic enzyme is one in animals, plants and fungi occurring enzyme, which catalyzes a key reaction for the provision of NADPH within the citrate shuttles. This malate is converted to pyruvate. This existing with one isoform in both mitochondria ( ME3 ) and in the cytosol (ME1 ) enzyme is found in humans in all tissue types. Plants also have two isoforms.

In addition to the NADP -dependent malic enzyme, there are Malatenzyme that function with NAD: firstly, the NAD-dependent malic enzyme ( decarboxylating oxaloacetate ) is reduced in the NAD ( EC 1.1.1.38 ). Again, oxaloacetate can serve as a substrate. On the other hand, there is also an NAD -dependent malate enzyme, which also uses NAD is reduced ( EC 1.1.1.39 ), but oxaloacetate can not be implemented. Malate enzymes are not the same as the malate dehydrogenase!

Catalyzed reaction

NADP NADPH CO2

L- malate is decarboxylated to pyruvate, with the generation of a NADPH from NADP a. Oxaloacetate is also accepted as a substrate.

Generation of NADPH

Occurring in the pentose phosphate pathway in addition to the enzyme glucose-6 -phosphate dehydrogenase, 6 -phosphogluconate dehydrogenase, and a shape of the isocitrate dehydrogenase, the NADP -dependent malic enzyme for animals is the only way to generate NADPH.

Protein isoform Decarboxylation Oxaloacetic acid Phosphogluconate dehydrogenase (decarboxylating) Digital Object Identifier Biochimica et Biophysica Acta
541748
de