Ki for (AMP) in ATP regeneration from AMP with ADP intermediate

Value 40 uM
Organism Corn Zea mays
Reference Hatch M. D., Properties and Regulation of Adenylate Kinase from Zea mays Leaf Operating in C, Pathway Photosynthesis, Aust. J. Plant Physiol., 1982, 9, 287-96
Method For the direction towards ADP formation, activity was measured as NADH oxidation at 340 nm in reactions containing enzyme, 25 mM HEPES-KOH buffer, pH 7.8 or as specified, 2 mM ATP, 0.5 mM AMP, 2.5 mM MgCl, and a coupling system consisting of 3 units of pyruvate kinase, 5 units of lactate dehydrogenase, 0.5 mM PEP, 0.25 mM NADH and 30 mM KC1 in a total volume of 1 ml.
Comments AMP strongly inhibited the reverse direction reaction, acting in a strictly competitive manner with respect to ADP
Entered by Uri M
ID 103414