Description
A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another.
Abbr
L-LDH, Native (Bovine)
Applications
For use in enzymatic determination of lactate or pyruvate.
Form
Type I, Suspension in 2.2 M ammonium sulfate; Type II, buffered aqueous glycerol solution, Solution in 50% glycerol containing 0.025 M potassium phosphate buffer, pH 7.5; Type III, ammonium sulfate suspension, Crystalline suspension in 2.1 M (NH4)2SO4 solution, pH 6.0; Type IV, buffered aqueous glycerol solution, Solution in 50% glycerol containing 0.025 M potassium phosphate buffer, pH 7.5.
Enzyme Commission Number
EC 1.1.1.27
Activity
>90%. (>200U/mL)
Unit Definition
One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37°C.
Pathway
Cysteine and methionine metabolism, organism-specific biosystem; Glycolysis / Gluconeogenesis, organism-specific biosystem; Propanoate metabolism, organism-specific biosystem
Function
L-lactate dehydrogenase activity
Synonyms
EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate
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