Inhibitors | Comment | Organism | Structure |
---|---|---|---|
NADP+ 2',3'-dialdehyde | irreversible inactivation in absence of substrate. The inactivation is first order with respect to NADP+ concentration and follows saturation kinetics, indicating that the enzyme initially forms a reversible complex with the inhibitor followed by covalent modification. NADP+ and NAD+ protect the enzyme from inactivation. One molecule of NADP+ 2',3'-dialdehyde binds per subunit of glucose-6-phosphate dehydrogenase when the enzyme is completely inactivated | Leuconostoc mesenteroides |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
200 | - |
NADP+ 2',3'-dialdehyde | 25°C, pH 7.8 | Leuconostoc mesenteroides |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Leuconostoc mesenteroides | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glucose 6-phosphate + NADP+ 2',3'-dialdehyde | - |
Leuconostoc mesenteroides | 6-phospho-D-glucono-1,5-lactone + NADPH 2',3'-dialdehyde + H+ | - |
? |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
1.8 | - |
NADP+ 2',3'-dialdehyde | 25°C, pH 7.8 | Leuconostoc mesenteroides |