49971
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:
MDL number:
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
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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
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
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
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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