L9636
D-Lactic Dehydrogenase from Staphylococcus epidermidis
lyophilized powder, ≥80 units/mg solid
Synonyme(s) :
Lactate, (R)-Lactate:NAD+ oxidoreductase, D-LDH
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About This Item
Produits recommandés
Source biologique
bacterial (Staphylococcus epidermidis)
Niveau de qualité
Forme
lyophilized powder
Activité spécifique
≥80 units/mg solid
Température de stockage
−20°C
Description générale
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.
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.
Actions biochimiques/physiologiques
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.
Définition de l'unité
One unit will reduce 1.0 μmole of pyruvate to D-lactate per min at pH 7.0 at 25 °C.
Forme physique
Lyophilized powder containing primarily dextran
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
Certificats d'analyse (COA)
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E M Barnes et al.
Proceedings of the National Academy of Sciences of the United States of America, 66(4), 1190-1198 (1970-08-01)
The transport of beta-galactosides by isolated membrane preparations from Escherichia coli strains containing a functional y gene is markedly stimulated by the conversion of D-lactate to pyruvate. The addition of D-lactate to these membrane preparations produces a 19-fold increase in
Mechanisms of active transport in isolated membrane vesicles. II. The mechanism of energy coupling between D-lactic dehydrogenase and beta-galactoside transport in membrane preparations from Escherichia coli.
H R Kaback et al.
The Journal of biological chemistry, 246(17), 5523-5531 (1971-09-10)
Biochemistry, lactate dehydrogenase
Farhana A and Lappin SL
StatPearls [Internet] (2020)
Lactate dehydrogenase D is a general dehydrogenase for D-2-hydroxyacids and is associated with D-lactic acidosis
Jin S, et al.
Nature Communications, 14(1), 6638-6638 (2023)
Enzymatic characterization of D-lactate dehydrogenase and application in alanine aminotransferase activity assay kit
Sun Y, et al.
Bioengineered, 12(1), 6459-6471 (2021)
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