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Literature summary for 2.6.1.16 extracted from
- Isomerase activity of the C-terminal fructose-6-phosphate binding domain of glucosamine-6-phosphate synthase from Escherichia coli (2001), J. Enzyme Inhib., 16, 373-380.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 3.8 | - |
D-fructose 6-phosphate | pH 7.2, 37°C, isomerization catalyzed by C-terminal domain | Escherichia coli |  |
| 16 | - |
D-glucose 6-phosphate | pH 7.2, 37°C, isomerization catalyzed by C-terminal domain | Escherichia coli | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
HB101 strain | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-fructose 6-phosphate | isomerase activity studied over C-terminal D-fructose 6-phosphate binding domain constituted by residues 241 to 608 | Escherichia coli | D-glucose 6-phosphate | - |
r | |
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