L9636
D-Lactic Dehydrogenase from Staphylococcus epidermidis
lyophilized powder, ≥80 units/mg solid
Synonym(s):
Lactate, (R)-Lactate:NAD+ oxidoreductase, D-LDH
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biological source
bacterial (Staphylococcus epidermidis)
Quality Level
form
lyophilized powder
specific activity
≥80 units/mg solid
storage temp.
−20°C
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.[1] D-Lactic Dehydrogenase (LDHD) codes for D-isomer and is highly expressed in tissues characterized by high metabolic rates and abundant mitochondria.[2]
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.[1] D-Lactic Dehydrogenase (LDHD) codes for D-isomer and is highly expressed in tissues characterized by high metabolic rates and abundant mitochondria.[2]
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. [3]
D-Lactic Dehydrogenase from Staphylococcus epidermidis has been used in the analysis of D-lactic acid.[4]
Biochem/physiol Actions
Lactate dehydrogenase (LDH) plays an important role in the anaerobic metabolic pathway.[1] The mammalian lactate dehydrogenase D (LDHD) is responsible for catalyzing the conversion of D-lactate to pyruvate.[2] D-lactate dehydrogenase (D-LDH) is commonly employed in clinical settings for the detection of alanine aminotransferase (ALT) activity.[7] Mutations in LDHD found in patients with D-lactic acidosis result in reduced LDHD activity.[2]
Unit Definition
One unit will reduce 1.0 μmole of pyruvate to D-lactate per min at pH 7.0 at 25 °C.
Physical form
Lyophilized powder containing primarily dextran
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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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)
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
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)
C C Taylor et al.
Journal of dairy science, 85(7), 1793-1800 (2002-08-31)
Chopped barley forage was ensiled untreated or treated with several doses (1 x 10(5) to 1 x 10(6) cfu/g of fresh forage) of Lactobacillus buchneri 40788 in laboratory silos and untreated or treated (4 x 10(5) cfu/g) in a farm
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