|
( Lactate dehydrogenase)
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+. At high concentrations of lactate, the enzyme exhibits feedback inhibition and the rate of conversion of pyruvate to lactate is decreased. It also catalyzes the dehydrogenation of 2-Hydroxybutyrate, but it is a much poorer substrate than lactate. There is little to no activity with beta-hydroxybutyrate. The five isozymes that are usually described in the literature each contain four subunits. The major isozymes of skeletal muscle and liver, M4, has four muscle (M) subunits; while H (heart)4 is the main isozymes for heart muscle in most species, containing 4 H subunits. The other variants contain both types of subunits.
|
Lactate dehydrogenase Subcategories
Lactate dehydrogenase Articles
|
| 
