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Results 1 - 10 of 19 > >>
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EC Number Cofactor Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP - 660567, 660682, 660791, 660803, 660948, 661013, 661073, 661135, 661266, 661558, 661746, 661759, 662153, 662154, 662180, 662206, 662212, 662279, 662302, 662321, 662347, 662378, 662380, 662386, 662393, 662452, 662491, 662614, 662674, 662675, 662681, 662708, 662709, 662851, 662873, 663212, 663236, 663237, 663295, 663349, 663394, 671598, 671678, 672227, 672647, 672829, 673601, 673866, 674837, 675021, 675598, 675671, 675892, 676192, 677061, 677184, 690339, 690353, 690366, 690540, 691022, 691092, 691139, 691722, 692133, 692138, 692212, 692216, 692294, 692313, 692515, 692602, 693043, 693123, 693126, 693198, 693206, 693219, 693323, 693735, 693742, 693925, 694153, 694155, 694186, 694279, 694375, 694404, 694508, 708764, 710100, 710589, 721548, 721663, 721701, 721744, 722670, 722805, 722989, 723596
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP as MgATP2- 661884
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP as MgATP2-, binding site structure 662608
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP binding mechanism 661314
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP binding pocket and small lobe structure, binding involves D166, N171, D184, and K72 663344
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP binding site structure: spans both lobes, the N-terminal beta-sheet and C-terminal alpha-helix of the core scaffold, binding of ATP and release of ADP in the open enzyme conformation, residues Asp184, Lys72, and Asp166 are involved, schematic overview 490800
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP binds between two lobes, directing the gamma-phosphate outwards while the adenine ring lies deep in the cleft between the lobes 660951
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP dependent on, the binding site is a deep pocket lined by hydrophobic residues, enzyme affinity for ATP is increased 2fold by phosphorylation of the activation loop at THr197, ATP competes with the phosphorylated activation loop, that acts as an autoinhibitory substrate 490935
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP optimal at 0.0025 mM, binding involves phosphorylation of Thr197 661480
Display the word mapDisplay the reaction diagram Show all sequences 2.7.11.11ATP PKA-Mg2+-ATP-substrate complex formation and effects on enzyme activity and stability, overview 677019
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