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Merck

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

CAS Number:
9028-36-8
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-829-0
MDL number:
MFCD00130907
EC Number:
1.1.1.28 (BRENDA, IUBMB)
Specific activity:
150-500 units/mg protein
Biological source:
bacterial (Lactobacillus leichmannii)

Key Documents

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biological source

bacterial (Lactobacillus leichmannii)

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

Quality Level

200

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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.

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

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.
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.

Physical form

Lyophilized powder containing phosphate buffer salts

Other Notes

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.

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

L3888-5KU: + L3888-BULK: + L3888-500UN-PW: + L3888-500UN: + L3888-2.5KU: + L3888-VAR: + L3888-2.5KU-PW:

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Certificates of Analysis (COA)

Lot/Batch Number
0000452305
0000452304
0000452305
0000452304
0000438448

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Biosynthesis and Activity of Prenylated FMN Cofactors
Wang PH, et al.
Cell Chemical Biology, 25(5), 560-570 (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)
Structural Insights into Mdn1, an Essential AAA Protein Required for Ribosome Biogenesis
Chen Z, et al.
Cell, 175(3), 822?834-822?834 (2018)
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)
Biochemistry, Lactate Dehydrogenase
Farhana A and Lappin SL
StatPearls [Internet] (2023)
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