EC Number | Crystallization (Comment) | Organism |
---|---|---|
5.3.1.9 | enzyme complexed with the competitive inhibitor D-gluconate 6-phosphate, X-ray crystallography at 2.5 A resolution | Oryctolagus cuniculus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
5.3.1.9 | D-gluconate 6-phosphate | - |
Oryctolagus cuniculus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
5.3.1.9 | cytoplasm | - |
Oryctolagus cuniculus | 5737 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.3.1.9 | D-glucose 6-phosphate | Oryctolagus cuniculus | in the cytoplasm, it catalyzes the second step in glycolysis. Outside the cell, it serves as a nerve growth factor and cytokine | D-fructose 6-phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.3.1.9 | Oryctolagus cuniculus | Q9N1E2 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.3.1.9 | D-glucose 6-phosphate | the active site residues Lys58 and His388 might be involved in catalytic mechanism | Oryctolagus cuniculus | D-fructose 6-phosphate | - |
? | |
5.3.1.9 | D-glucose 6-phosphate | in the cytoplasm, it catalyzes the second step in glycolysis. Outside the cell, it serves as a nerve growth factor and cytokine | Oryctolagus cuniculus | D-fructose 6-phosphate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
5.3.1.9 | dimer | the enzyme is a dimer with two alpha/beta-sandwich domains in each subunit | Oryctolagus cuniculus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
5.3.1.9 | autocrine motility factor | - |
Oryctolagus cuniculus |
5.3.1.9 | Neuroleukin | - |
Oryctolagus cuniculus |