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49971

Sigma-Aldrich

D-Lactic Dehydrogenase from Lactobacillus leichmannii

suspension, yellow, ~1000 U/mL

Synonyme(s) :

(R)-Lactate:NAD+ oxidoreductase, D-Lactate Dehydrogenase

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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

Source biologique

bacterial (Lactobacillus leichmannii)

Forme

suspension

Activité spécifique

≥30 U/mg protein

Concentration

~1000 U/mL

Impuretés

L-Lactat Dehydrogenase, none detected
3.2 M Ammonium sulfate solution (pH ~6.2)

Couleur

yellow

Température de stockage

2-8°C

Application

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.

Actions biochimiques/physiologiques

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.
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.

Définition de l'unité

1 U corresponds to the amount of enzyme which will reduce 1 μmol of pyruvate to D-lactate per minute at pH 7.0 and 25 °C

Forme physique

only partially soluble in water or buffer

Remplacé(e)(s) par

Réf. du produit
Description
Tarif

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves

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Certificats d'analyse (COA)

Lot/Batch Number

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Takenori Satomura et al.
Journal of bioscience and bioengineering, 106(1), 16-21 (2008-08-12)
Dye-linked D-lactate dehydrogenase activity was found in the crude extract of a continental thermoacidophilic crenarchaeota, Sulfolobus tokodaii strain 7, and was purified 375-fold through four sequential chromatography steps. With a molecular mass of about 93 kDa, this enzyme was a
Svetlana V Antonyuk et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 65(Pt 12), 1209-1213 (2010-01-08)
The crystal structure of D-lactate dehydrogenase from Aquifex aeolicus (aq_727) was determined to 2.12 A resolution in space group P2(1)2(1)2(1), with unit-cell parameters a = 90.94, b = 94.43, c = 188.85 A. The structure was solved by molecular replacement
Judith Wienstroer et al.
FEBS letters, 586(1), 36-40 (2011-12-14)
D-Lactate negatively affects Arabidopsis thaliana seedling development in a concentration-dependent manner. At media D-lactate concentrations greater than 5-10mM the development of wild-type plants is arrested shortly after germination whereas plants overexpressing the endogenous D-lactate dehydrogenase (D-LDH) detoxify D-lactate to pyruvate
Ting-Ting Xu et al.
Applied biochemistry and biotechnology, 160(2), 314-321 (2008-06-25)
The low-energy nitrogen ion beam implantation technique was used in the breeding of mutant D(-)-lactic-acid-producing strains. The wild strain Sporolactobacillus sp. DX12 was mutated by an N(+) ion beam with energy of 10keV and doses ranging from 0.4 x 10(15)
A N Minenko et al.
Biochemistry. Biokhimiia, 71(1), 32-38 (2006-02-07)
Mammalian cytochrome P450scc (CYP11A1p) is a pseudointegral protein of the inner membrane of mitochondria with the active center exposed in the matrix. Upon import of the CYP11A1p precursor into yeast mitochondria, only a minor part was incorporated into the inner
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