EC Number   |
Reaction |
Reference |
|---|
   2.7.1.170 | ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O = ADP + N-acetylmuramate 6-phosphate |
- |
- |
| 2.7.1.170 | ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O = ADP + N-acetylmuramate 6-phosphate |
catalytic mechanism, molecular docking, dynamics simulation |
-, 738937 |
| 2.7.1.170 | ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O = ADP + N-acetylmuramate 6-phosphate |
reaction mechanism, structure-function analysis, overview. A one-step catalytic mechanism is proposed that involves attack of water at the anomeric center leading to cleavage of the 1,6-anhydro ring and phosphoryl transfer. The reaction inverts the anomeric center of MurNAc. Transient formation of an intermediate (MurNAc) in a two-step mechanism may also be possible. It is also possible that the gamma-phosphate leaves the ATP as a transient metaphosphate prior to the anhydro-bond cleavage |
738636 |
| 2.7.1.170 | ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O = ADP + N-acetylmuramate 6-phosphate |
the oxygen of 1,6-anhydro-N-acetyl-beta-muramate, that is to be phosphorylated, is trapped in the anhydro ring structure and must first be cleaved prior to phosphorylation. In order to do this, Asp182 is predicted to act as a base to deprotonate a water molecule and enhance its nucleophilicity. The water would then attack the anomeric carbon of the sugar concomitant with transfer of the gamma-phosphate of ATP. The lone pair electrons from the O5 position would assume partial double-bond characteristics and stabilize the oxocarbenium ion that would otherwise develop, with the anomeric carbon adopting an axial conformation in the product acetylmuramate 6-phosphate, catalytic role of the conserved residue Asp182 residue in catalysis |
738435 |
