Phosphoenolpyruvate carboxylase: Difference between revisions

Revision as of 15:24, 1 August 2019

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.

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 01-August-2019

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
5fdn – PEPC 3 + aspartate + citrate – Arabidopsis thaliana
5vyj – PEPC + glycine - corn

ReferencesReferences

↑ 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
↑ 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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

[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

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[2]

@@ Line 6: / Line 6: @@
 == Structural highlights ==
-Maze PEPC <scene name='57/573979/Cv/2'>active site</scene> contains an <scene name='57/573979/Cv/3'>Mn+2 ion</scene><ref>PMID:12467579</ref>. <scene name='57/573979/Cv/4'>Aspartate binding site</scene>. Water molecules shown as red spheres.
+Maze PEPC <scene name='57/573979/Cv/2'>active site</scene> contains an <scene name='57/573979/Cv/3'>Mn+2 ion</scene><ref>PMID:12467579</ref>. <scene name='57/573979/Cv/5'>Aspartate binding site</scene>. Water molecules are shown as red spheres.
 </StructureSection>
 ==3D structures of phosphoenolpyruvate carboxylase==