EC Number   |
Reaction |
Reference |
|---|
   5.4.99.9 | UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose |
- |
- |
| 5.4.99.9 | UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose |
catalytic mechanism, overview |
-, 727319 |
| 5.4.99.9 | UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose |
catalytic reaction mechanism, detailed overview. A covalent adduct is formed between the substrate and the FADH cofactor, temporarily breaking the glycosidic bond, followed by an internal proton transfer between N5FADH and O6FADH. The next step involves linearization of the sugar and formation of the iminium ion species. In the next step, the sugar cyclizes into its five-membered ring form. This step is isotope sensitive and is considered to be the chemical rate-limiting step of the mechanism. Once the furanose form of the sugar is reached, another internal proton transfer takes place, and the glycosidic bond to UDP is formed. Finally, the product of the reaction exits the active site of the enzyme |
747150 |
| 5.4.99.9 | UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose |
chemical reaction mechanism, overview |
-, 726820 |
| 5.4.99.9 | UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose |
detailed reaction mechanism involving SN2-type steps, overview |
747461 |
| 5.4.99.9 | UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose |
enzyme-substrate binding structure and mechanism |
748028 |
| 5.4.99.9 | UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose |
mobile loop of enzyme must move in order for enzyme to bind UDP-galactose substrate |
678290 |
| 5.4.99.9 | UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose |
quantum mechanics-molecular mechanics (QM/MM) molecular dynamics study and reaction mechanism, characterization of the structures of reactants, products, intermediate species and transitions states, overview |
749138 |
| 5.4.99.9 | UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose |
reaction mechanism including FAD cofactor, overview. Role of a covalent flavin N5 intermediate in the isomerization, non-redox reaction, of UDP-galactopyranose (UDP-Galp) to UDP-galactofuranose (UDP-Galf) by UDP-galactopyranose mutase (UGM). The flavin is required to be in the reduced state and functions as a nucleophile. The flavin must cycle back to the oxidized state for sustained catalysis. Formation of a N5-iminium ion intermediate, Fformation of N5-adducts in non-redox reactions involving the flavin in the oxidized or reduced forms |
746922 |
| 5.4.99.9 | UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose |
reaction mechanism, overview. FAD-UDP-alpha-D-galactopyranose/UDP-alpha-D-galactofuranose adduct as an intermediate in the catalytic cycle, the chemical mechanism for UGM involves an SN2-type displacement of UDP from UDP-alpha-D-galactopyranose/UDP-alpha-D-galactofuranose by N5 of FADred |
727937 |
