Phosphoenolpyruvate carboxykinase: Difference between revisions

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{{STRUCTURE_2olr|  PDB=2olr  | SIZE=350| SCENE= |right|CAPTION=ATP-driven E. coli PEPCK complex with ATP (stick model), CO2 and Mg+2 ion (green)  [[2olr]] }}


<StructureSection load='1khf' size='350' side='right' caption='GTP-driven E. coli PEPCK complex with PEP (stick model), ethanediol, Na+ and Mn+2 ions (green) (PDB entry [[1khf]])' scene=''>
__TOC__
== Function ==
'''Phosphoenolpyruvate carboxykinase''' (PEPCK) catalyzes the conversion of oxaloacetate to phosphoenolpyruvate (PEP) and CO<sub>2</sub>.  PEPCK is part of the gluconeogenesis pathway<ref>PMID:9242918</ref>.  There are 3 types of PEPCK distinguished by the energy source of the reaction which can be GTP, ATP or diphosphate.
'''Phosphoenolpyruvate carboxykinase''' (PEPCK) catalyzes the conversion of oxaloacetate to phosphoenolpyruvate (PEP) and CO<sub>2</sub>.  PEPCK is part of the gluconeogenesis pathway<ref>PMID:9242918</ref>.  There are 3 types of PEPCK distinguished by the energy source of the reaction which can be GTP, ATP or diphosphate.


== Structural highlights ==
''E. coli'' GTP-driven PEPCK active site is located in a pocket at the enzyme surface<ref>PMID:11851336</ref>.
</StructureSection>
== 3D Structures of PEPCK ==
== 3D Structures of PEPCK ==


Revision as of 11:19, 27 June 2016

Function

Phosphoenolpyruvate 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 highlights

E. coli GTP-driven PEPCK active site is located in a pocket at the enzyme surface[2].


GTP-driven E. coli PEPCK complex with PEP (stick model), ethanediol, Na+ and Mn+2 ions (green) (PDB entry 1khf)

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3D Structures of PEPCK3D Structures of PEPCK

Updated on 27-June-2016

ReferencesReferences

  1. ↑ 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
  2. ↑ 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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Michal Harel, Jaime Prilusky, Alexander Berchansky, Joel L. Sussman
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