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49971

Sigma-Aldrich

D-Lactic Dehydrogenase from Lactobacillus leichmannii

suspension, yellow, ~1000 U/mL

Synonym(s):

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

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About This Item

CAS Number:
9028-36-8
Enzyme Commission number:
1.1.1.28 (BRENDA, IUBMB)
MDL number:
MFCD00130907
UNSPSC Code:
12352204

biological source

bacterial (Lactobacillus leichmannii)

form

suspension

specific activity

≥30 U/mg protein

concentration

~1000 U/mL

impurities

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

color

yellow

storage temp.

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.

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.
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

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

Physical form

only partially soluble in water or buffer

replaced by

Product No.
Description
Pricing

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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.

EU REACH Annex XVII (Restriction List)

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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
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
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)
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
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