Article
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused desensitization and abolished responsiveness to regulatory phosphorylation.
The Journal of biological chemistry - 25 Mar 2005
Takahashi-Terada Akiko, Kotera Masaaki, Ohshima Kenta, Furumoto Tsuyoshi, Matsumura Hiroyoshi, Kai Yasushi, Izui Katsura
Abstract excerpt
Phosphoenolpyruvate carboxylases (PEPC, EC 4.1.1.31) from higher plants are regulated by both allosteric effects and reversible phosphorylation. Previous x-ray crystallographic analysis of Zea mays PEPC has revealed a binding site for sulfate ion, speculated to be the site for an allosteric activator, glucose 6-phosphate (Glc-6-P) (Matsumura, H., Xie, Y., Shirakata, S., Inoue, T., Yoshinaga, T., Ueno, Y., Izui,...
Topics
- Amino Acid Sequence
- Binding Sites
- Enzyme Activation
- Glucose-6-Phosphate
- Molecular Sequence Data
- Mutation
- Phosphoenolpyruvate Carboxylase
- Phosphorylation
- Protein Structure, Secondary
- Sulfates
- Zea mays