Description
In enzymology, a D-lactate dehydrogenase is an enzyme that catalyzes the chemical reaction: (D)-lactate + 2 ferricytochrome c↔ pyruvate + 2 ferrocytochrome c. Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD.
Abbr
D-LDH, Native (Lactobacillus delbrückii)
Source
Lactobacillus delbrückii
Applications
Use D-Lactate Dehydrogenase (D-LDH), Grade II, in a variety of diagnostic tests, e.g., in the determination of alanine aminotransferases, lactate or pyruvate. Used for the removal of pyruvate in determinations working with NADH (i.e., triglycerides, lipase, aldolase, aspartate aminotransferases, glutamate dehydrogenase).
Appearance
White to yellowish lyophilizate
Product Overview
Dehydrogenase that catalyzes the interconversion of D(-)-lactate to pyruvate. Rely on the proven diagnostic quality of this product.
Contaminants
Alcohol dehydrogenase: <0.01 GIucose dehydrogenase: <0.01 Malate dehydrogenase: <0.1 Succinate dehydrogenase: <0.01
Michaelis Constant
D-lactate: 0.7 x 10-1 mol/l (NAD, 2 mmol/l) Pyruvate: 1.2 x 10-3 mol/l (NADH, 0.1 mmol/l) NADH: 7.1 x 10-5 mol/l (pyruvate, 20 mmol/l)
Specificity
Lactate dehydrogenase is specific for D(–)-lactate, L(+)-lactate does not react.
Thermal stability
Up to +50°C
Stability
At +2 to +8°C within specification range for 12 months. Store dry.
Synonyms
D-Lactic Dehydrogenase; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(−)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(−)-lactic cytochrome c reductase
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