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L2011

Sigma-Aldrich

D-Lactic Dehydrogenase from Lactobacillus leichmannii

ammonium sulfate suspension, ≥250 units/mg protein (biuret)

Synonyme(s) :

Lactate, (R)-Lactate:NAD+ oxidoreductase, D−LDH

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About This Item

Numéro CAS:
9028-36-8
Numéro de classification (Commission des enzymes):
1.1.1.28 (BRENDA, IUBMB)
Numéro MDL:
MFCD00130907
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Forme

ammonium sulfate suspension

Niveau de qualité

200

Activité spécifique

≥250 units/mg protein (biuret)

Activité étrangère

Malic dehydrogenase <0.5% of base activity

Température de stockage

2-8°C

Description générale

Research area: Cell Signalling D-lactate dehydrogenase belongs to the D-isomer-specific 2-hydroxyacid dehydrogenase family. Lactate dehydrogenase (LD) is a tetramer consisting of two (H and M) subunits. It has five isozymes (LD1 to LD5) and this composition varies in different tissues. LD1 is abundant in the kidney, heart, and erythrocytes. LD5 is found in the liver and skeletal muscles. LD is a ubiquitous molecule found in plants, yeast, mammals, and microorganisms and is a member of the oxidoreductase family.

Actions biochimiques/physiologiques

Lactic dehydrogenase (LDH)plays an important role in the glycolytic pathway where it converts pyruvate tolactate by using NAD+ as a co-factor. It is considered animportant molecule that can be used in cancer therapy as it acts as aglycolytic inhibitor. Inhibition of LDH is associated with blocking of aerobicglycolysis in tumour cells.

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

Suspension in 3.2 M (NH4)2SO4, pH 6.0

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

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H Taguchi et al.
The Journal of biological chemistry, 266(19), 12588-12594 (1991-07-05)
The gene encoding D-lactate dehydrogenase (D-lactate: NAD+ oxidoreductase, EC 1.1.1.28) of Lactobacillus plantarum has been sequenced, and expressed in Escherichia coli cells with an inducible expression plasmid, in which the 5'-noncoding region of the gene was replaced with the tac
Torben Larsen
Analytical biochemistry, 539, 152-157 (2017-11-06)
D-lactic acid in the mammalian body is mainly of microbiological origin and is often located somewhere along the digestive tract. Surgical, extensive re-sectioning of the small bowel may be one of the risk factors for altered balance in the microbiological
C L McLaughlin et al.
Journal of dairy science, 92(6), 2758-2766 (2009-05-19)
A challenge model was used to evaluate a new approach to controlling acute acidosis. Acute acidosis reduces performance in both dairy and beef cattle and most often occurs as a consequence of ingestion of large amounts of readily fermentable starch
Zhaojuan Zheng et al.
Applied and environmental microbiology, 78(9), 3480-3483 (2012-02-22)
NAD-dependent l- and d-lactate dehydrogenases coexist in Lactobacillus genomes and may convert pyruvic acid into l-lactic acid and d-lactic acid, respectively. Our findings suggest that the relative catalytic efficiencies of ldhL- and ldhD-encoded products are crucial for the optical purity
Wenwen Zhao et al.
Analytical chemistry, 84(15), 6701-6706 (2012-07-04)
We proposed the first application of an electrophoretically mediated microanalysis (EMMA) method for fast online discrimination and determination of substrate enantiomers, which was achieved by just one EMMA assay. Lactate dehydrogenase (LDH)-catalyzed reaction was studied to evaluate the feasibility and
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