Sandbox GGC13

Crystal Structure of Lactate Dehydrogenase A

spinqualitylabelsall models Crystal Structure L-Lactate Dehydrogenase A interacting with inhibitor, Oxamate Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D This is a default text for your page Sandbox GGC13. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Function Lactate Dehydrogenase is a large, two domain- protein which catalyzes the conversion of pyruvate to lactate under anaerobic conditions. This conversion is coupled with the reduction of NAD+ to form the electron carrying NADH. Muscular lactate dehydrogenase is involved in the Cori Cycle where it transports newly synthesized lactate to the liver. Liver lactate dehydrogenase converts the lactate back to pyruvate in order to provide the precursor for gluconeogenesis. Structural highlights Lactate dehydrogenase is a tetramer protein which can form five different isoenzymes. Lactate dehydrogenase subunits exist primarily in two isoforms: M and H, which differ in a single residue. The M subunit contains an alanine while the H subunit contains a glutamine. The combination of subunits defines which isoenzyme is formed and indicates where the enzyme will be present in the body. Lactate dehydrogenase A is composed of four M subunits. The subunits can adopt two conformations, open and closed, which determine the subunits activity. Interactions between the A-chain subunit and the inhibitor, oxamate. The substrate active site to which oxamate is bound is in the closed conformation. This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.