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Malate Dehydrogenase

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malate dehydrogenase [′ma‚lāt dē′hī·drə·jə‚nās]
(biochemistry)

Malate Dehydrogenase 

an enzyme of the oxidoreductase class widely distributed in animal and plant cells, where it catalyzes the dehydrogenation of malic acid to oxalacetic acid in the tricarboxylic acid cycle. In higher plants and animals there are two different malate dehydrogenases, one localized in the mitochondria and the other in the soluble fraction of the cell.

Decarboxylating malate dehydrogenase (malic enzyme) catalyzes the readily reversible formation reaction of malic acid from pyruvic acid and CO2, as well as the decarboxylation of oxalacetic acid.



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All fish were screened for two polymorphic protein-coding muscle loci: malate dehydrogenase (sMDH-3) and general muscle protein (PROT-3).
mentella: malate dehydrogenase mobility patterns compared with extrinsic gasbladder muscle passages and anal fin ray counts.
Of the enzyme systems initially assayed, alcohol dehydrogenase (ADH); lactate dehydrogenase (LDH); malate dehydrogenase (MDH); phosphohexose isomerase (PHI/PGI); and 6-phosphogluconate dehydrogenase (6-PGD) resolved consistently.
 
 
 
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