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 active site contains an Mn+2 ion[2].

3D structures of phosphoenolpyruvate carboxylase

Updated on 29-August-2017

3odm – PEPC + malonate – Clostridium perfringens
3zgb, 3zge – PEPC + aspartate – Flaveria pringlei
1fiy, 1qb4 – EcPEPC + aspartate – Escherichia coli
1jqn – EcPEPC + aspartate + PEP analog
1jqo – PEPC – corn
4bxc – FtPEPC + α-D-glucose-6-phosphate – Flaveria trinervia
4bxh – FtPEPC

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