ATP, ADP and AMP on the regulation of lactate dehydrogenase activity of Phycomyces blakesleeanus.
1. The inhibition of ATP, ADP and AMP on lactate dehydrogenase activity from Phycomyces blakesleeanus was investigated kinetically at pH 6.0 and 7.5. 2. At pH 6.0 ATP was more effective as inhibitor than ADP and AMP. 3. All three nucleotides bind cooperatively to the enzyme, ATP and ADP decrease the positive homotropic interactions of NADH at pH 6.0. 4. The results obtained may contribute to explain the regulation of lactate dehydrogenase from Phycomyces blakesleeanus at acid pH values.
D000244:Adenosine Diphosphate / Q000494:pharmacology*; D000249:Adenosine Monophosphate / Q000494:pharmacology*; D000255:Adenosine Triphosphate / Q000494:pharmacology*; D005658:Fungi / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000037:antagonists & inhibitors*; D009243:NAD / Q000378:metabolism; D010800:Phycomyces / Q000201:enzymology*
D009243:NAD; D000249:Adenosine Monophosphate; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D007770:L-Lactate Dehydrogenase