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 I, 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. Benefit from the extended shelf life of this enzyme.
Contaminants
Alcohol dehydrogenase: <0.01 Malate dehydrogenase: <0.1 "NADH oxidase": <0.0005 Succinate dehydrogenase: <0.01 NH4: <0.01 μmol/KU Na (flame photometric): <0.5 μmol/KU K (flame photometric): <0.007 μmol/KU
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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