2.7.11.2	ATP	-	660805, 660923, 661046, 661094, 661812, 661961, 661963, 662151, 662397, 662537, 662948, 671870, 672273, 672978, 673007, 673647, 674640, 674730, 677167, 698954, 705630, 721523, 721971, 722148, 722788, 723006	
2.7.11.2	ATP	binding kinetics, ATP or ADP plus pyruvate at low concentration of about 0.1 mM cause PDHK2 dimer to associate to a tetramer. These changes make major contributions to synergistic inhibition of PDHK2 activity by ADP and pyruvate, overview	674544	
2.7.11.2	ATP	binding site structure, involves Gly317 and Tyr320, and K+ ions	661219	
2.7.11.2	ATP	binding structure with isozyme PDK4, detailed overview	721159	
2.7.11.2	ATP	causes a decrease in PDHK2 affinity for the L2 domain	660995	
2.7.11.2	ATP	dependent on	348935, 640580, 642132, 642133, 642134, 642135, 642136, 642137, 642138, 642139, 642141, 642142, 642143, 642144, 642145, 642146, 642148, 642149, 642150, 642151, 642152, 642153, 642154, 642155, 642156, 642157, 642158, 642159, 642160, 642162, 642163, 642164, 642165, 94884, 94893	
2.7.11.2	ATP	L2 binding increases affinities for both ADP and ATP	661592	
2.7.11.2	ATP	ordered reaction mechanism with ATP	661094	
2.7.11.2	ATP	the ATP-binding loop in one PDHK3 subunit adopts an open conformation, implying that the nucleotide loading into the active site is mediated by the inactive pre-insertion binding mode	675449	
2.7.11.2	ATPgammaS	dissociation constants as ATP in binding to PDK3	661592	
2.7.11.2	additional information	no activation by Ca2+/calmodulin or calmodulin alone	642138	
2.7.11.2	additional information	no activation by cAMP	642133, 642136, 642137, 642138	
2.7.11.2	additional information	no activation by cGMP	642136, 642137, 642138	
2.7.11.2	additional information	no activation by succinyl-CoA, tiglyl-CoA, crotonyl-CoA, glutaryl-CoA, DL-3-hydroxy-3-methylglutaryl-CoA, acetylcarnitine or 3-hydroxybutyryl-CoA	642139	
2.7.11.2	additional information	no activity with GTP	660995