FunctionPhosphoenolpyruvate carboxykinase (PEPCK) catalyzes the conversion of oxaloacetate to phosphoenolpyruvate (PEP) and CO2. PEPCK is part of the gluconeogenesis pathway[1]. There are 3 types of PEPCK distinguished by the energy source of the reaction which can be GTP, ATP or diphosphate.
Structural highlightsE. coli GTP-driven PEPCK is located in a pocket at the enzyme surface[2]. Water molecules are shown as red spheres.
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3D Structures of PEPCK3D Structures of PEPCK
Updated on 01-August-2019
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- Phosphoenolpyruvate carboxykinase ATP driven
- 1oen, 1fiy – EcPEPCK - Escherichia coli
- 6crt – EcPEPCK (mutant) + ATP + Mn
- 6cu4 – EcPEPCK (mutant) + pyruvate + Ca
- 1ayl – EcPEPCK + ATP + oxalate + Mg
- 1aq2 – EcPEPCK + ATP + pyruvate + Mg + Mn
- 2py7 – EcPEPCK (mutant) + ATP + Mg + Mn
- 6d5i – EcPEPCK (mutant) + ATP + pyruvate + Mn
- 2olq – EcPEPCK + ATP + CO2 + Mg + Mn
- 2pxz – EcPEPCK + ATP + CO2 + oxaloacetate + Mg + Mn
- 2olr – EcPEPCK + ATP + CO2 + Mg
- 1os1 – EcPEPCK + ATP + pyruvate + Mg + Ca
- 6com – EcPEPCK (mutant) + ATP + pyruvate + Mg + Ca
- 1k3c – EcPEPCK + ADP + pyruvate + Mg + AlF3
- 1k3d – EcPEPCK + ADP + Mg + AlF3
- 1j3b – TtPEPCK – Thermus thermophilus
- 1yvy – AnsPEPCK – Anaerobiospirillum succiniciproducens
- 1ytm – AnsPEPCK + ATP + oxalate + Mg + Mn
- 1xkv, 2pc9 – TtPEPCK + ATP
- Phosphoenolpyruvate carboxykinase GTP driven
- 1khf – EcPEPCK + PEP + Mn
- 1khg – EcPEPCK + Mn
- 1m51, 1nhx – EcPEPCK + inhibitor + Mn
- 2faf – cPEPCK + Mn - chicken
- 2qzy – cPEPCK + PEP + Mn
- 2gmv – hPEPCK + inhibitor + PEP + Mn - human
- 2qew – rPEPCK + Mn - rat
- 5v95 – rPEPCK (mutant) + Mn
- 2qf1 – rPEPCK + oxaloacetate + Mn
- 2rk7, 4ywb – rPEPCK + oxalate + Mn
- 2rk8, 2rka, 2rkd, 2rke, 4yw8, 4ywd – rPEPCK + inhibitor + Mn
- 4wiu – MtPEPCK + oxalate + Mn – Mycobacterium tuberculosis
- 4wie – MtPEPCK + Mn
- 4wpt – MtPEPCK + PEP
- 4wpv – MtPEPCK (mutant) + Pi + Zn
- PEPCK GTP driven complex with nucleotide
- 1khb – EcPEPCK + GTP analog + Mg
- 1khe – EcPEPCK + GTP analog + Mn
- 2fah – cPEPCK + GDP + Mn
- 2qey – rPEPCK + GTP + Mn
- 5fh0, 5fh1, 5fh2, 5v97 – rPEPCK (mutant) + Mn + GTP
- 4gnm, 4gnq - rPEPCK + oxalate + GTP + Mn
- 4gmw, 4gnl, 4gnp – rPEPCK + PEP + GDP + Mn
- 3dt2, 3dt4, 4gmu – rPEPCK + GTP + oxalate + Mn
- 3mof, 5fh3, 5v9g – rPEPCK (mutant) + GTP + oxalate + Mn
- 3dt7, 4gmm, 4gmz, 4gno – rPEPCK + GTP + sulfopyruvate + Mn
- 3moe, 4ox2, 5fh4, 5v9f – rPEPCK (mutant) + GTP + sulfopyruvate + Mn
- 3dtb – rPEPCK + GTP + phosphoglycolate + Mn
- 3moh, 5fh5, 5v9h – rPEPCK (mutant) + GDP + phosphoglycolate + Mn
- 2qf2 – rPEPCK + GDP + oxaloacetate + Mn
- 4yw9 – rPEPCK + inhibitor + Mn + GTP
- 4rcg – MtPEPCK + GDP + Mg
- 4r43 – MtPEPCK + GDP + Mn
- 5i67 – MtPEPCK (mutant) + Mn + GDP
- 4wl8 – MtPEPCK + Mn + GTP analog
- 4wou – MtPEPCK + Mn + Zn + GDP
- 4wpu – MtPEPCK (mutant) + PEP + GDP
- PEPCK
- 2zci – PEPCK – Corynebacterium glutamicum
- 1ygg – AsPEPCK – Actinobacillus succinogenes
- 1ylh – AsPEPCK + pyruvate + Mn
- 1ii2 – PEPCK – Trypanosoma cruzi
ReferencesReferences
- ↑ Hanson RW, Reshef L. Regulation of phosphoenolpyruvate carboxykinase (GTP) gene expression. Annu Rev Biochem. 1997;66:581-611. PMID:9242918 doi:http://dx.doi.org/10.1146/annurev.biochem.66.1.581
- ↑ Dunten P, Belunis C, Crowther R, Hollfelder K, Kammlott U, Levin W, Michel H, Ramsey GB, Swain A, Weber D, Wertheimer SJ. Crystal structure of human cytosolic phosphoenolpyruvate carboxykinase reveals a new GTP-binding site. J Mol Biol. 2002 Feb 15;316(2):257-64. PMID:11851336 doi:http://dx.doi.org/10.1006/jmbi.2001.5364
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