Phosphoenolpyruvate carboxylase

From Proteopedia

spinqualitylabelsall models Structure of E. coli phosphoenolpyruvate carboxylase complex with PEP analog, aspartate and Mn+2 ion (green) (PDB entry 1jqn) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Phosphoenolpyruvate carboxylase (PEPC) catalyzes the addition of bicarbonate to phosphoenolpyruvate to form oxaloacetate and phosphate. PEPC is part of the carbon fixation process in plants[1]. PEPC is inhibited by aspartate, fumarate and malonate. Structural highlights Maze PEPC contains an [2]. . Water molecules are shown as red spheres.

3D structures of phosphoenolpyruvate carboxylase

Updated on 22-September-2020

3zgb, 3zge – PEPC + aspartate – Flaveria pringlei
1jqo – cPEPC – corn
5vyj – cPEPC + glycine
6u2t – cPEPC + malate
6mgi – cPEPC + α-D-glucose-6-phosphate
4bxc – FtPEPC + α-D-glucose-6-phosphate – Flaveria trinervia
4bxh – FtPEPC
5fdn – PEPC 3 + aspartate + citrate – Arabidopsis thaliana
3odm – PEPC + malonate – Clostridium perfringens
1fiy, 1qb4 – EcPEPC + aspartate – Escherichia coli
1jqn – EcPEPC + aspartate + PEP analog

References

1. ↑ Rademacher T, Hausler RE, Hirsch HJ, Zhang L, Lipka V, Weier D, Kreuzaler F, Peterhansel C. An engineered phosphoenolpyruvate carboxylase redirects carbon and nitrogen flow in transgenic potato plants. Plant J. 2002 Oct;32(1):25-39. PMID:12366798
2. ↑ Matsumura H, Xie Y, Shirakata S, Inoue T, Yoshinaga T, Ueno Y, Izui K, Kai Y. Crystal structures of C4 form maize and quaternary complex of E. coli phosphoenolpyruvate carboxylases. Structure. 2002 Dec;10(12):1721-30. PMID:12467579