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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In this study, malate dehydrogenase, pyruvate kinase, and G6PDH dehydrogenase activity was not affected by dietary CBH levels, indicating that the glycolytic pathway and pentose phosphate pathway are not affected by the level of dietary CBH in Litopenaeus vannamei at low salinities.
14) (Cytidylate kinase) 1459 Q9XSJ4 Alpha-enolase (NNE) 2049 Q3T145 Malate dehydrogenase, cytoplasmic 1141 P50454 Collagen-binding protein 2 precursor 2956 Q3T149 Heat-shock protein beta-1 (HSPB1) 453 P04272 Annexin A2 (Annexin II) 2068 Q61792 LIM and SH3 domain protein 1 (LASP-1) 3308 Q71FK5 Actin, cytoplasmic 1 (Beta-actin) Spot Protein Protein Sequence Total Fold No (MW) (PI) coverage ion score change * (%) C.
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.
The sequences for phosphoenolpyruvate carboxykinase (PEPCK), malate dehydrogenase (MD), and fumarate reductase (FR) were also obtained.
3-phosphoglycerol dehydrogenase and malate dehydrogenase (8).
neomexicanus also has been documented through allozyme electrophoretic analyses of several populations in New Mexico; Parker and Selander (1984) found only two clones based upon a malate dehydrogenase locus among 112 specimens from seven localities and Cole et al.