Lactate Dehydrogenase: Difference between revisions

{{STRUCTURE_2a92|  PDB=2a92  | SIZE=400| SCENE= |right|  CAPTION=Lactate dehydrogenase tetramer complex with NADH, [[2a92]] }}

<scene name='Jasper_Small_Lactate_Sandbox_1/Basic/1'>Lactate Dehydrogenase (LDH)</scene> is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvate were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+.   

[[1kbj]] - LDH FMN-binding domain