EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.1.3.11 | G191A | decreased Km-value for fructose 1,6-diphosphate, decreased inhibition constant for fructose 1,6-diphosphate and decreased Mg2+ affinity compared to the wild type enzyme. The 50% inhibiting concentration of AMP is increased over 2000fold relative to the wild type enzyme, loss of AMP cooperativity, mechanism of AMP inhibition changes from competitive to noncompetitive | Sus scrofa |
3.1.3.11 | I190T | decreased Km-value for fructose 1,6-diphosphate, decreased inhibition constant for fructose 1,6-diphosphate decreased Mg2+ affinity compared to the wild type enzyme. The 50% inhibiting concentration of AMP is increased over 2000fold relative to the wild type enzyme, loss of AMP cooperativity, mechanism of AMP inhibition changes from competitive to noncompetitive | Sus scrofa |
3.1.3.11 | K42E | decreased Km-value for fructose 1,6-diphosphate, decreased inhibition constant for fructose 1,6-diphosphate and decreased Mg2+ affinity compared to the wild type enzyme. The 50% inhibiting concentration of AMP is increased over 2000fold relative to the wild type enzyme, loss of AMP cooperativity | Sus scrofa |
3.1.3.11 | K42T | decreased Km-value for fructose 1,6-diphosphate, decreased inhibition constant for fructose 1,6-diphosphate decreased Mg2+ affinity compared to the wild type enzyme. The 50% inhibiting concentration of AMP is increased over 2000fold relative to the wild type enzyme, loss of AMP cooperativity, mechanism of AMP inhibition changes from competitive to noncompetitive | Sus scrofa |
3.1.3.11 | Q32L | decreased Km-value for fructose 1,6-diphosphate and decreased inhibition constant for fructose 1,6-diphosphate compared to the wild type enzyme. 1.7fold increase in turnover number, 8fold increase in Mg2+ affinity. 8fold increase in 50% inhibiting concentration of AMP | Sus scrofa |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.3.11 | 0.00084 | - |
fructose 1,6-diphosphate | mutant enzyme G191A | Sus scrofa | |
3.1.3.11 | 0.00142 | - |
fructose 1,6-diphosphate | mutant enzyme Q32L | Sus scrofa | |
3.1.3.11 | 0.00153 | - |
fructose 1,6-diphosphate | mutant enzyme K42T | Sus scrofa | |
3.1.3.11 | 0.00167 | - |
fructose 1,6-diphosphate | mutant enzyme K42E | Sus scrofa | |
3.1.3.11 | 0.00181 | - |
fructose 1,6-diphosphate | mutant enzyme I190T | Sus scrofa | |
3.1.3.11 | 0.00351 | - |
fructose 1,6-diphosphate | wild type enzyme | Sus scrofa |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.3.11 | Sus scrofa | P00636 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.1.3.11 | wild type and mutant enzymes | Sus scrofa |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.3.11 | D-fructose 1,6-diphosphate + H2O | - |
Sus scrofa | D-fructose 6-phosphate + phosphate | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.1.3.11 | 2.3 | - |
fructose 1,6-diphosphate | mutant enzyme G191A | Sus scrofa | |
3.1.3.11 | 18 | - |
fructose 1,6-diphosphate | wild type enzyme | Sus scrofa | |
3.1.3.11 | 18.3 | - |
fructose 1,6-diphosphate | mutant enzyme K42T | Sus scrofa | |
3.1.3.11 | 19.3 | - |
fructose 1,6-diphosphate | mutant enzyme K42E | Sus scrofa | |
3.1.3.11 | 21.1 | - |
fructose 1,6-diphosphate | mutant enzyme I190T | Sus scrofa | |
3.1.3.11 | 32.1 | - |
fructose 1,6-diphosphate | mutant enzyme Q32L | Sus scrofa |