Crystallization (Comment) | Organism |
---|---|
H188N mutant with bound GDP-perosamine, to 1.7 A resolution. The sugar analog is trapped in the active site as an external aldimine. The active site is positioned between the two subunits of the dimer. The diphosphoryl groups of the ligand are anchored to the protein via Arg219 and Arg331, the hydroxyl groups of the hexose only lie within hydrogen bonding distance to ordered water molecules. The hexose moiety of the ligand adopts a boat rather than the typically observed chair conformation | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
H188K | mutant protein cannot catalyze the dehydration step | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | Q9F118 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
GDP-4-dehydro-alpha-D-rhamnose + L-glutamate | - |
Escherichia coli | GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + 2-oxoglutarate + ammonia | - |
? | |
GDP-D-perosamine + L-glutamate | - |
Escherichia coli | GDP-4-dehydro-3,6-dideoxymannose + 2-oxoglutarate + ammonia | wild-type ColD is able to catalyze the production of GDP-4-keto-3,6-dideoxymannose using GDP-perosamine instead of GDP-4-keto-6-deoxymannose as a substrate | ? |