Malate Dehydrogenase

Cat. No.

CED018

Product Overview

Malate Dehydrogenase produced in microorganism has a molecular mass of 34 kDa .

Description

Malate dehydrogenase is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of malate to pyruvate producing NADPH.Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses the inner mitochondrial membrane. Once in the cytosol, the malate is oxidized back to oxaloacetate by cytosolic malate dehydrogenase. Finally, phosphoenol-pyruvate carboxy kinase (PEPCK) converts oxaloacetate to phosphoenol pyruvate.

Synonyms

malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate (NAD) dehydrogenase; NAD-dependent malate dehydrogenase; NAD-specific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; (S)-malate:NAD+ oxidoreductase.

Appearance

White amorphous powder, lyophilized

Molecular Weight

34 kDa

Isoelectic  point

4.9

Michealis constants

2.5×10-5M (NADH) 2.0×10-5M (Oxaloacetate) 

Inhibitors

Ag⁺,Hg²⁺

pH Stability

4.0~8.0

Optimum pH

9.0

Optimum Temperature

55℃

Specific activity

≥ 200U/mg protein

Unit definition

One unit will cause the oxidation of one micromole NADH per min at pH 7.5 at 30℃.

Thermal Stability

< 60℃ (pH7.5, 15min)

Preparation Instructions

The enzyme is reconstituted in 100mM potassium phosphate buffer, pH 7.5 containing 0.2% BSA for activity assay.