An iso-random Bi Bi mechanism for adenylate kinase.
An iso-random Bi Bi mechanism has been proposed for adenylate kinase. In this mechanism, one of the enzyme forms can bind the substrates MgATP and AMP, whereas the other form can bind the products MgADP and ADP. In a catalytic cycle, the conformational changes of the free enzyme and the ternary complexes are the rate-limiting steps. The AP(5)A inhibition equations derived from this mechanism show theoretically that AP(5)A acts as a competitive inhibitor for the forward reaction and a mixed noncompetitive inhibitor for the backward reaction.
Sheng
X R
XR
National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, 100101, China.
Li
X
X
Pan
X M
XM
D000249:Adenosine Monophosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000263:Adenylate Kinase / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D002384:Catalysis; D007700:Kinetics; D008956:Models, Chemical
D000249:Adenosine Monophosphate; D000255:Adenosine Triphosphate; D000263:Adenylate Kinase