LP15033-1

Lactate dehydrogenase

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Descriptions

Lactate dehydrogenase (LDH) is an enzyme (EC 1.1.1.27) present in a wide variety of organisms, including plants and animals. It catalyses the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+. As it can also catalyze the oxidation of hydroxybutyrate, it is occasionally called hydroxybutyrate dehydrogenase (HBD). Copyright Text is available under the Creative Commons Attribution/Share-Alike License. See http://creativecommons.org/licenses/by-sa/3.0/ for details. Source: Wikipedia, D-lactate (Wikipedia)

Lactate dehydrogenase (LDH, or also called LD) is an oxidoreductase (LD: EC 1.1.1.27) and is the most important clinically of several dehydrogenases occurring in human serum. LDH catalyses the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD. When disease, injury, or toxic material damages tissues, cells release LDH into the bloodstream. Since LDH is a fairly stable enzyme, it has been widely used to evaluate the presence of damage and toxicity of tissue and cells. LDH is cytoplasmic in its cellular location and in any one tissue is composed of one or two of five possible isoenzymes. While many of its clinical applications involve quantification of one or more specific serum isoenzymes, an estimate of total LDH is usually required. Lactate dehydrogenase catalyzes the reversible reaction: L-lactate + NAD <--> pyruvate + NADH. Testing methods either measure the increase in NADH produced in the lactate-to-pyruvate reaction or the decrease in NADH produced in the pyruvate-to-lactate reaction. PMID: 3882046. Reference ranges are highly method dependent. The pyruvate-to-lactate reaction is preferred theoretically because the equilibrium constant is large and the rate for any amount of enzyme is 2-3 times faster, thus smaller sample and shorter observation periods are needed. Disadvantages of the pyruvate-to-lactate reaction are loss of linearity as compared with the lactate-to-pyruvate reaction, and greater substrate inhibition of the enzyme. [Tietz Fourth Edition] Source: Regenstrief LOINC

Basic Part Properties

Part Display Name

Lactate dehydrogenase

Part Type

Component (Describes the core component or analyte measured)

Created On

2000-05-04

Construct for LOINC Short Name

LDH

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