Phosphoenolpyruvate carboxylase: Difference between revisions
Jump to navigation
Jump to search
Michal Harel (talk | contribs) No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
<StructureSection load='1jqn' size=' | <StructureSection load='1jqn' size='400' side='right' caption='Structure of E. coli phosphoenolpyruvate carboxylase complex with PEP analog, aspartate and Mn+2 ion (green) (PDB entry [[1jqn]])' scene='57/573979/Cv/1' pspeed='8'> | ||
== Function == | == Function == |
Revision as of 15:26, 29 August 2017
FunctionPhosphoenolpyruvate 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 highlightsMaze PEPC active site contains an Mn+2 ion[2]. |
|
3D structures of phosphoenolpyruvate carboxylase3D 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
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