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Literature summary for 3.5.99.6 extracted from
- Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution (1995), Structure, 3, 1323-1332.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| structure of the enzyme in complexes with its allosteric activator and with a competitive inhibitor | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3 | the mechanism comprises steps to open the pyranose ring of the substrate and a sequence of general base-catalyzed reactions to bring about isomerization and deamination, with Asp72 playing a key role as a proton exchanger | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glucosamine 6-phosphate + H2O | - |
Escherichia coli | D-fructose 6-phosphate + NH3 | - |
? |  |
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