EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
2.7.1.1 | 3-phosphoglycerate | activates | Saccharomyces cerevisiae | |
2.7.1.1 | citrate | allosteric activator | Saccharomyces cerevisiae | |
2.7.1.1 | phosphate | activates | Saccharomyces cerevisiae |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.7.1.1 | D-mannose | competitive to D-glucose | Saccharomyces cerevisiae |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.1.1 | Saccharomyces cerevisiae | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.7.1.1 | kinetic-based biospecific affinity chromatographic studies | Saccharomyces cerevisiae |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.7.1.1 | ATP + D-hexose = ADP + D-hexose 6-phosphate | random process | Saccharomyces cerevisiae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.1.1 | D-glucose + ATP | - |
Saccharomyces cerevisiae | ADP + D-glucose 6-phosphate | - |
? | |
2.7.1.1 | D-mannose + ATP | - |
Saccharomyces cerevisiae | ADP + D-mannose 6-phosphate | - |
? | |
2.7.1.1 | additional information | allosteric enzyme, catalyzes phosphoryl transfer from MgATP2- to the 6-OH group of a number of furanose- and pyranose-type compounds | Saccharomyces cerevisiae | ? | - |
? |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.1.1 | 25 | - |
assay at | Saccharomyces cerevisiae |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.7.1.1 | 7.5 | - |
assay at | Saccharomyces cerevisiae |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.7.1.1 | ATP | activates, ATP-dependent enzyme | Saccharomyces cerevisiae |