EC Number |
Reaction |
Reference |
---|
2.7.2.3 | ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate |
active site structure containing 2 tryptophan residues, substrate binding |
642241 |
2.7.2.3 | ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate |
an ordered mechanism is assumed where 3-phospho-D-glycerate and 3-phospho-D-glyceroyl phosphate bind before ADP and ATP, respectively |
-, 724980 |
2.7.2.3 | ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate |
C-terminal part is important for full activity |
642282 |
2.7.2.3 | ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate |
catalytic mechanism and cycle, conformational changes for substrate binding and positioning, overview |
738225 |
2.7.2.3 | ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate |
mechanism |
642251, 642252, 642288, 642301 |
2.7.2.3 | ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate |
mechanism, substrate-induced effects combine synergistically to induce major conformational changes of the active site to catalytic status |
642286 |
2.7.2.3 | ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate |
Pro204 is important for stability and catalytic mechanism of the enzyme |
642293 |
2.7.2.3 | ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate |
random sequential mechanism |
642168 |
2.7.2.3 | ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate |
rapid equilibrium random mechanism |
642247, 642259 |
2.7.2.3 | ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate |
residues engaged in 3-phospho-D-glycerate binding: R22, D24, R144, E149, E150, H191, R192, residues engaged in ATP binding: G236, G237, G263, G371, G375, P372, E277, E377, G407, G408, G429-431 |
-, 642281 |