Application

Lactic Dehydrogenase, recombinant fromE. coli has been used:in lactate dehydrogenase (LDH) and malate dehydrogenase 1 (MDH1)assays and cross-linking assaysto prepare assay buffer to measure pyruvate kinase (PYK) by coupled assayin in vitro DltC D-alanylation assay

Biochem/physiol Actions

Conversion of L-lactate into L-pyruvate is crucial in hypoxic and anaerobic conditions, especially when synthesis of adenosine triphosphate (ATP) by oxidative phosphorylation is interrupted.

L-lactic dehydrogenase catalyzes the conversion of L-lactate into L-pyruvate while reducing NAD⁺ to NADH and H⁺.

General description

LDH (lactic dehydrogenase), a glycolytic enzyme, particularly present in skeletal muscle, heart, liver, kidneys, brain, lungs and red blood cells. It has five isoenzyme forms. LDH possess a tetrameric structure.

Unit Definition

One unit corresponds to the amount of enzyme which reduces 1 µmol pyruvate per minute at pH 7.4 and 25°C (NADH as cofactor)