L3888
D-Lactic Dehydrogenase from Lactobacillus leichmannii
lyophilized powder, 150-500 units/mg protein
Synonym(s):
(R)-Lactate:NAD+ oxidoreductase, D-LDH
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About This Item
biological source
bacterial (Lactobacillus leichmannii)
Quality Level
form
lyophilized powder
specific activity
150-500 units/mg protein
composition
Protein, ~50% biuret
foreign activity
Malic dehydrogenase <0.5% of base activity
storage temp.
−20°C
General description
Research area: Cell Signaling
Lactate Dehydrogenase (LDH) is classified as an oxidoreductase and is found in various organisms, including both plants and animals. LDH is widely distributed across all tissues, with high concentrations in muscle, kidney, and liver. The genes encoding LDH are LDHA, LDHB, LDHC, and LDHD. The D-isomer is produced by LDHD. There are two types of D-LDHs: NAD-dependent D-LDHs and FAD-dependent D-LDHs.
Lactate Dehydrogenase (LDH) is classified as an oxidoreductase and is found in various organisms, including both plants and animals. LDH is widely distributed across all tissues, with high concentrations in muscle, kidney, and liver. The genes encoding LDH are LDHA, LDHB, LDHC, and LDHD. The D-isomer is produced by LDHD. There are two types of D-LDHs: NAD-dependent D-LDHs and FAD-dependent D-LDHs.
Application
D-Lactic Dehydrogenase from Lactobacillus leichmannii has been used:
- in lactate dehydrogenase activity for testing the chaperone activity of proteins
- to test the kinase activities of purified thiamine monophosphate(ThiM)
- in NADH-coupled steady-state ATPase assay
- to determine cellular lactate
In the food industry, the primary catalysis is coupled to conversion of NADH and H+ to NAD+ with diaphorase coupled with converting the non-fluorescent resazurin to the highly fluorescent substance resorufin to measure the content of D-lactate in food products.
Biochem/physiol Actions
It acts as a crucial checkpoint in gluconeogenesis and DNA metabolism. Elevated levels of LDH in the blood have been observed in various conditions, including heart attacks, cancers, liver disease, muscle trauma, anemia, bone fractures, and infections such as encephalitis, human immunodeficiency virus(HIV), and meningitis. LDH also serves as a non-specific marker of tissue turnover, which is a normal metabolic process. Additionally, reduced D-LDH activity has been found in case of mutations in LDHD found in patients with D-lactic acidosis.
D-lactic dehydrogenase catalyzes the conversion of pyruvate into D-lactate, with oxidation of NADH to NAD+. D-lactic dehydrogenase can also catalyze the reverse reaction, conversion of D-lactate into pyruvate with reduction of NAD+ to NADH.
Unit Definition
D-lactic dehydrogenase catalyzes the conversion of pyruvate into D-lactate, with oxidation of NADH to NAD+. D-lactic dehydrogenase can also catalyze the reverse reaction, conversion of D-lactate into pyruvate with reduction of NAD+ to NADH.
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 phosphate buffer salts
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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Find documentation for the products that you have recently purchased in the Document Library.
Biochemistry, Lactate Dehydrogenase
Farhana A and Lappin SL
StatPearls [Internet] (2023)
Lactate dehydrogenase D is a general dehydrogenase for D-2-hydroxyacids and is associated with D-lactic acidosis
Shan J, et al.
Nature Communications, 14, 6638-6638 (2023)
A Novel Method for Assessing the Chaperone Activity of Proteins
Hristozova N, et al.
PLoS ONE, 11(8), e0161970-e0161970 (2016)
Structural Insights into Mdn1, an Essential AAA Protein Required for Ribosome Biogenesis
Chen Z, et al.
Cell, 175(3), 822?834-822?834 (2018)
Cysteine Deprivation Targets Ovarian Clear Cell Carcinoma Via Oxidative Stress and Iron?Sulfur Cluster Biogenesis Deficit
Novera W, et al.
Antioxidants & Redox Signaling, 33(17), 1191?1208-1191?1208 (2020)
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