Phosphoenolpyruvate carboxylase

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. PEPC is inhibited by aspartate, fumarate and malonate.

Structural highlights

Maze PEPC active site contains an Mn+2 ion^[1].

Structure of E. coli phosphoenolpyruvate carboxylase complex with PEP analog, aspartate and Mn+2 ion (green) (PDB entry 1jqn)

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3D structures of phosphoenolpyruvate carboxylase3D structures of phosphoenolpyruvate carboxylase

Updated on 27-June-2016

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

ReferencesReferences

↑ 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

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Michal Harel, Alexander Berchansky, Joel L. Sussman, Lucas Xavier da Cunha, Karsten Theis

[1] 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

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