Protein Variants | Comment | Organism |
---|---|---|
K107M | 46fold increase in Ki-value for naphthyl 2,6-bisphosphate, 11.5fold increase in KM-value for D-fructose 1,6-diphosphate. The structure of the enzyme is isomorphous with respect to wild-type enzyme | Oryctolagus cuniculus |
K146M | decrease in rate of complex formation between enzyme and inhibitor 1-hydroxy-2-naphthaldehyde 6-phosphate, but no change in ability to form the complex | Oryctolagus cuniculus |
S271 | mutation decreases by 1 order of magnitude the affinity of 1-hydroxy-2-naphthaldehyde 6-phosphate for the aldolase active site but does not modify its ability to catalyze Schiff base formation | Oryctolagus cuniculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
1-hydroxy-2-naphthaldehyde 6-phosphate | slow-binding | Oryctolagus cuniculus | |
naphthyl 2,6-bisphosphate | competitive | Oryctolagus cuniculus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.013 | - |
D-fructose 1,6-bisphosphate | wild-type enzyme | Oryctolagus cuniculus | |
0.15 | - |
D-fructose 1,6-bisphosphate | mutant enzyme K107M | Oryctolagus cuniculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | P00883 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
muscle | - |
Oryctolagus cuniculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-fructose 1,6-bisphosphate | - |
Oryctolagus cuniculus | glycerone phosphate + D-glyceraldehyde 3-phosphate | - |
? |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00028 | - |
naphthyl 2,6-bisphosphate | wild-type enzyme | Oryctolagus cuniculus | |
0.013 | - |
naphthyl 2,6-bisphosphate | mutant enzyme K107M | Oryctolagus cuniculus | |
0.125 | - |
1-hydroxy-2-naphthaldehyde 6-phosphate | wild-type enzyme | Oryctolagus cuniculus |