EC Number |
Reaction |
Reference |
---|
2.7.1.107 | ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate |
- |
- |
2.7.1.107 | ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate |
analysis of the catalytic kinase mechanism molecular dynamics and quantum mechanics calculations, and density functional theory calculations, overview. The active site is relatively open and able to accommodate ligands in multiple orientations, suggesting that the optimization of binding orientations and conformational changes occurs prior to actual phosphoryl transfer |
739255 |
2.7.1.107 | ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate |
analysis of the catalytic mechanism using crystal structure anaysis, structure-function analysis, mutagenesis studies, molecular dynamics simulations, and density functional theory modelling, overview |
739145 |
2.7.1.107 | ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate |
C-terminal active site comprises residues 371-501, the C1 domain is absolutely required for catalytic activity, residues Asp434, Asp650, Asp465, and Asp497 are involved |
660956 |
2.7.1.107 | ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate |
catalytic and regulatory mechanisms |
-, 661157 |
2.7.1.107 | ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate |
conserved residues in the extended cysteine-rich domain CRD are essential for activity. e.g. G236, P244, and P245 |
661229 |
2.7.1.107 | ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate |
random equilibrium mechanism |
640387 |