Regulation of lactate dehydrogenase activity: reversible and isoenzyme-specific inhibition of the tetramerization process by peptides.
The transition of inactive lactic dehydrogenase (LDH) subunits to functional tetramers is controlled by 2 naturally-occurring peptides. One of these peptides inhibits the folding/association/activation process of H-LDH and the other peptide, the reconstitution of M-LDH, NADH and NAD+ are isoenzyme-specific antagonists of the 2 inhibitory peptides.
D004789:Enzyme Activation / Q000187:drug effects; D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase / Q000037:antagonists & inhibitors*; D046911:Macromolecular Substances; D009243:NAD / Q000494:pharmacology; D010455:Peptides / Q000494:pharmacology*; D011487:Protein Conformation / Q000187:drug effects
D007527:Isoenzymes; D046911:Macromolecular Substances; D010455:Peptides; D009243:NAD; D007770:L-Lactate Dehydrogenase