Dogfish M4 lactate dehydrogenase: reversible inactivation by pyridoxal 5'-phosphate and complete protection in complexes that mimic the active ternary complex.
Dogfish M4 lactate dehydrogenase, like the corresponding pig enzyme, is inactivated by pyridoxal 5'-phosphate through modification of a single essential lysine residue. The activity is completely protected in the complexes E-NAD+-oxalate, E-NADH-oxamate and E-(NAD+-pyruvate adduct), but only partially protected in E-NAD+, E-NADH, E-NAD+-oxamate and E-NADH-oxalate.
D000818:Animals; D004284:Dogfish; D007527:Isoenzymes; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000037:antagonists & inhibitors*; D008239:Lysine; D009243:NAD; D010070:Oxalates; D010072:Oxamic Acid; D011732:Pyridoxal Phosphate / Q000494:pharmacology*
D007527:Isoenzymes; D010070:Oxalates; D009243:NAD; D011732:Pyridoxal Phosphate; D007770:L-Lactate Dehydrogenase; D008239:Lysine; D010072:Oxamic Acid