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General description
Research Area: Cell Signaling
Lactate dehydrogenase (LDH), a cytoplasmic enzyme, belongs to the class of oxidoreductases. It is found in almost all tissues particularly high concentrations in muscle, liver, and kidney. Moderate concentrations of this enzyme are also present in red blood cells. LDH is comprised of five isomeric forms that come together in tetramers made up of either muscle (M) or heart (H) subunits. D-Lactic Dehydrogenase (LDHD) codes for D-isomer and is highly expressed in tissues characterized by high metabolic rates and abundant mitochondria.
Application
D-Lactic Dehydrogenase can be used to generate inhibitors of angiotensin converting enzyme by catalyzing the production of the intermediate (R)-2-Hydroxy-4-phenylbutyric acid.
D-Lactic Dehydrogenase from Staphylococcus epidermidis has been used in the analysis of D-lactic acid.
D-Lactic dehydrogenase has been used in a study to assess mechanisms of active transport in isolated membrane vesicles. It has also been used in a study to investigate β-galactoside transport in bacterial membrane preparations.
Biochem/physiol Actions
Lactate dehydrogenase (LDH) plays an important role in the anaerobic metabolic pathway. The mammalian lactate dehydrogenase D (LDHD) is responsible for catalyzing the conversion of D-lactate to pyruvate. D-lactate dehydrogenase (D-LDH) is commonly employed in clinical settings for the detection of alanine aminotransferase (ALT) activity. Mutations in LDHD found in patients with D-lactic acidosis result in reduced LDHD activity.
Physical form
Lyophilized powder containing primarily dextran
Other Notes
One unit will reduce 1.0 μmole of pyruvate to
| biological source | bacterial (Staphylococcus epidermidis) |
| Quality Segment | 200 |
| form | lyophilized powder |
| specific activity | ≥80 units/mg solid |
| storage temp. | −20°C |
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