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.