EC Number   |
General Information |
Reference |
|---|
   5.4.2.4 | malfunction |
enzyme deletion disrupts PGAM1 activity and results in higher serine de novo synthesis flux |
748733 |
| 5.4.2.4 | metabolism |
NO may suppress 2,3-bisphospho-D-glycerate production by (1) inhibiting glyceraldehyde-3-phosphate dehydrogenase, the most critical glycolytic enzyme for the bioavailability of 1,3-bisphosphoglycerate, and to a lesser extent by (2) associated pH changes in the deoxy-hemoglobin-catalyzed depletion of nitrite, a metabolic reservoir of NO |
728236 |
| 5.4.2.4 | metabolism |
the enzyme primarily impacts 3-phosphoglycerate concentration and thereby serine pathway flux |
748733 |
| 5.4.2.4 | metabolism |
the main activity of the enzyme is synthase (EC 5.4.2.4), converting 1,3-bisphosphoglycerate to 2,3-bisphosphoglycerate. The second activity is mutase (phosphoglycerate mutase, EC 5.4.2.1), catalyzing the interconversion between 2-phosphoglycerate and 3-phosphoglycerate. The third activity is phosphatase (S-succinylglutathione hydrolase, EC 3.1.3.13), hydrolyzing 2,3-bisphosphoglycerate to 3-phosphoglycerate or 2-phosphoglycerate and phosphate |
728437 |
| 5.4.2.4 | more |
proposed mechanisms for the phosphatase and the synthase reactions involving residues His11 and Glu89 |
728437 |
| 5.4.2.4 | physiological function |
bisphosphoglycerate mutase is a multi-activity enzyme. Its main function is to synthesize the 2,3-bisphosphoglycerate, the allosteric effector of hemoglobin, the enzyme regulates 2,3-bisphosphoglycerate levels, quantum mechanics/molecular mechanics simulations based on the metadynamics and umbrella sampling simulations, detailed overview |
728437 |
| 5.4.2.4 | physiological function |
the enzyme is responsible for biosynthesis of 2,3-bisphospho-D-glycerate, which is an enhancer of oxygen off-loading from hemoglobin. It is very sensitive to changes in glycolytic rates because its synthesis by BPG synthase is dependent on the availability of the glycolytic intermediate 1,3-bisphosphoglycerate, metabolic enzyme regulation, overview |
728236 |
