Literature summary extracted from
Takahashi-Terada, A.; Kotera, M.; Ohshima, K.; Furumoto, T.; Matsumura, H.; Kai, Y.; Izui, K.
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused desensitization and abolished responsiveness to regulatory phosphorylation (2005), J. Biol. Chem., 280, 11798-11806.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
4.1.1.31 |
glucose 6-phosphate |
activates wild-type enzyme |
Zea mays |
|
4.1.1.31 |
glycine |
allosteric activator |
Zea mays |
|
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
4.1.1.31 |
- |
Zea mays |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
4.1.1.31 |
R183Q |
mutation results in complete desensitization to glucose 6-phosphate, heterotrophic effect of glucose 6-phosphate on the allosteric inhibitor L-malate is abolished. Sensitivity to the allosteric activator Gly is not affected |
Zea mays |
4.1.1.31 |
R183Q/R184Q |
mutation results in complete desensitization to glucose 6-phosphate |
Zea mays |
4.1.1.31 |
R184Q |
mutation results in complete desensitization to glucose 6-phosphate |
Zea mays |
4.1.1.31 |
R372Q |
mutation results in a marked decrease in sensitivity to glucose 6-phosphate |
Zea mays |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
4.1.1.31 |
L-malate |
inhibits wild-type enzyme |
Zea mays |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.1.1.31 |
Zea mays |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
4.1.1.31 |
recombinant |
Zea mays |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
4.1.1.31 |
phosphoenolpyruvate + HCO3- |
- |
Zea mays |
phosphate + oxaloacetate |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.1.1.31 |
PEPC |
- |
Zea mays |