[Non-linear, non-competitive inhibition of lactate dehydrogenase with carboxylic acid anions (substrate analogues)].
The carboxylic acid anions are shown to inhibit lactate dehydrogenase in a non-competitive manner at pH 8.5. The inhibitory effect of different carboxylates used increases in the direction acetate leads to formate leads to methacrylate. Non-competitive inhibition by carboxylates has a non-linear character with effective Hill exponent depending on the inhibitor concentration increasing to the value n approximately equal to 2 when inhibitor concentration increases. The kinetic model is proposed to account for non-linear non-competitive inhibition in consequence of the abortive ternary complexes formation in two enzyme conformations. The substrate analogues properties that result in non-competitive inhibition of lactatedehydrogenase are considered.
D000818:Animals; D002264:Carboxylic Acids / Q000494:pharmacology*; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000037:antagonists & inhibitors*; D009132:Muscles / Q000201:enzymology; D011485:Protein Binding; D013056:Spectrophotometry, Ultraviolet; D013329:Structure-Activity Relationship; D013552:Swine
D002264:Carboxylic Acids; D007770:L-Lactate Dehydrogenase
Nelineĭnoe nekonkurentnoe ingibirovanie laktatdegidrogenazy anionami karbonovykh kislot (analogami substrata).