EC Number | Cloned (Comment) | Organism |
---|---|---|
3.1.3.46 | as selenomethionine-substituted protein | Escherichia coli |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.1.3.11 | hanging drops in vapor diffusion, crystals of FBPase with citrate and fructose 2,6-bisphosphate | Escherichia coli |
3.1.3.11 | hanging drops in vapor diffusion, crystals of Zn2+/fructose 2,6-bisphosphate complex | Sus scrofa |
3.1.3.46 | as hanging drops in vapor diffusion VDX plates in complex with Mg2+ or Zn2+ and beta-D-fructose 2,6-bisphosphate | Sus scrofa |
3.1.3.46 | as hanging drops in vapor diffusion VDX plates with Mg2+, citrate and beta-D-fructose 2,6-bisphosphate | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.1.3.11 | AMP | AMP and D-fructose 2,6-bisphosphate are not synergistic inhibitors of the type I FBPase | Escherichia coli | |
3.1.3.11 | AMP | - |
Sus scrofa | |
3.1.3.11 | D-fructose 2,6-bisphosphate | AMP and fructose 2,6-bisphosphate are not synergistic inhibitors of the type I FBPase | Escherichia coli | |
3.1.3.11 | fructose 2,6-bisphosphate | global conformational change in porcine FBPase induced by fructose 2,6-bisphosphate in the absence of AMP | Sus scrofa | |
3.1.3.46 | AMP | beta-D-fructose 2,6-bisphosphate has no effect on AMP inhibition | Escherichia coli | |
3.1.3.46 | AMP | beta-D-fructose 2,6-bisphosphate enhances AMP inhibition | Sus scrofa |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.3.11 | Escherichia coli | P0A993 | - |
- |
3.1.3.11 | Sus scrofa | P00636 | - |
- |
3.1.3.46 | Escherichia coli | - |
- |
- |
3.1.3.46 | Sus scrofa | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.1.3.46 | by Cibacron Blue-Sepharose and Sephadex G-50 column chromatography | Escherichia coli |
3.1.3.46 | by Cibacron Blue-Sepharose and Sephadex G-50 column chromatography | Sus scrofa |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.1.3.46 | beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate | beta-D-fructose 2,6-bisphosphate induces a global conformational change in the absence of AMP | Sus scrofa | |
3.1.3.46 | beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate | the complex of E. coli FBPase with beta-D-fructose 2,6-bisphosphate remains in the R-state with dynamic loops in the engaged conformation | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.3.46 | beta-D-fructose 2,6-bisphosphate + H2O | - |
Escherichia coli | D-fructose 6-phosphate + phosphate | - |
? | |
3.1.3.46 | beta-D-fructose 2,6-bisphosphate + H2O | - |
Sus scrofa | D-fructose 6-phosphate + phosphate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.3.11 | type I FBPase | - |
Escherichia coli |
3.1.3.46 | 6-phosphofructo-2-kinase/fructose-2 6-biphosphatase | - |
Escherichia coli |
3.1.3.46 | 6-phosphofructo-2-kinase/fructose-2 6-biphosphatase | - |
Sus scrofa |
3.1.3.46 | FBPase | - |
Escherichia coli |
3.1.3.46 | FBPase | - |
Sus scrofa |