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 (Chicken)
Form
ammonium sulfate suspension; Crystalline suspension in 1.3 M (NH4)2SO4, pH 6.0
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.
Warnings
Protein determined by biuret.
Pathway
Cysteine and methionine metabolism, organism-specific biosystem; Glycolysis / Gluconeogenesis, organism-specific biosystem; Propanoate metabolism, organism-specific biosystem; Cysteine and methionine metabolism, organism-specific biosystem; Cysteine and methionine metabolism, conserved biosystem; Glycolysis / Gluconeogenesis, 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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