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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About This Item
Recommended Products
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. 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.
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.
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
Certificates of Analysis (COA)
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J M Neylon et al.
Journal of dairy science, 86(6), 2163-2169 (2003-07-03)
We studied the effect of increasing the cutting height of whole-plant corn at the time of harvest from 12.7 (NC) to 45.7 (HC) cm on yield and nutritive value of silage for dairy cows. Three leafy corn silage hybrids were
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
E Schmidt et al.
Journal of biotechnology, 24(3), 315-327 (1992-07-01)
(R)-2-Hydroxy-4-phenylbutyric acid, an intermediate in the manufacture of inhibitors of angiotensin converting enzyme, can be produced continuously in an enzyme membrane reactor by enzymatic reduction of its corresponding alpha-keto acid. D-Lactate dehydrogenase (D-LDH) from Staphylococcus epidermidis was chosen as the
Enzymatic characterization of D-lactate dehydrogenase and application in alanine aminotransferase activity assay kit
Sun Y, et al.
Bioengineered, 12(1), 6459-6471 (2021)
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)
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