Phosphoenolpyruvate carboxykinase: Difference between revisions

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== Function ==
== 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.
 
See also: [[Gluconeogenesis]].


== Structural highlights ==
== Structural highlights ==
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*<scene name='54/540171/Cv/10'>Mn coordination site</scene>.
*<scene name='54/540171/Cv/10'>Mn coordination site</scene>.
*<scene name='54/540171/Cv/11'>Na coordination site</scene>.
*<scene name='54/540171/Cv/11'>Na coordination site</scene>.
== 3D Structures of PEPCK ==
[[Phosphoenolpyruvate carboxykinase 3D structures]]


</StructureSection>
</StructureSection>
== 3D Structures of PEPCK ==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
*Phosphoenolpyruvate carboxykinase ATP driven
**[[1oen]], [[1fiy]] – EcPEPCK - ''Escherichia coli''<br />
**[[6crt]] – EcPEPCK (mutant) + ATP + Mn<br />
**[[6cu4]] – EcPEPCK (mutant) + pyruvate + Ca<br />
**[[1ayl]] – EcPEPCK + ATP + oxalate + Mg<br />
**[[1aq2]] – EcPEPCK + ATP + pyruvate + Mg + Mn<br />
**[[2py7]] – EcPEPCK (mutant) + ATP + Mg + Mn<br />
**[[6d5i]] – EcPEPCK (mutant) + ATP + pyruvate + Mn<br />
**[[2olq]] – EcPEPCK + ATP + CO2 + Mg + Mn<br />
**[[2pxz]] – EcPEPCK + ATP + CO2 + oxaloacetate + Mg + Mn<br />
**[[2olr]] – EcPEPCK + ATP + CO2 + Mg <br />
**[[1os1]] – EcPEPCK + ATP + pyruvate + Mg + Ca<br />
**[[6com]] – EcPEPCK (mutant) + ATP + pyruvate + Mg + Ca<br />
**[[1k3c]] – EcPEPCK + ADP + pyruvate + Mg + AlF3<br />
**[[1k3d]] – EcPEPCK + ADP + Mg + AlF3<br />
**[[1j3b]] – TtPEPCK – ''Thermus thermophilus'' <br />
**[[1yvy]] – AnsPEPCK – ''Anaerobiospirillum succiniciproducens''<br />
**[[1ytm]] – AnsPEPCK + ATP + oxalate + Mg + Mn<br />
**[[1xkv]], [[2pc9]] – TtPEPCK + ATP <br />
*Phosphoenolpyruvate carboxykinase GTP driven
**[[1khf]] – EcPEPCK + PEP + Mn <br />
**[[1khg]] – EcPEPCK + Mn <br />
**[[1m51]], [[1nhx]] – EcPEPCK + inhibitor + Mn<br />
**[[2faf]] – cPEPCK + Mn - chicken<br />
**[[2qzy]] – cPEPCK + PEP + Mn <br />
**[[2gmv]] – hPEPCK + inhibitor + PEP + Mn - human<br />
**[[2qew]] – rPEPCK + Mn - rat<br />
**[[5v95]] – rPEPCK (mutant) + Mn <br />
**[[2qf1]] – rPEPCK + oxaloacetate + Mn<br />
**[[2rk7]], [[4ywb]] – rPEPCK + oxalate + Mn<br />
**[[2rk8]], [[2rka]], [[2rkd]], [[2rke]], [[4yw8]], [[4ywd]] – rPEPCK + inhibitor + Mn<br />
**[[4wiu]] – MtPEPCK + oxalate + Mn – ''Mycobacterium tuberculosis''<br />
**[[4wie]] – MtPEPCK + Mn <br />
**[[4wpt]] – MtPEPCK + PEP <br />
**[[4wpv]] – MtPEPCK (mutant) + Pi + Zn <br />
*PEPCK GTP driven complex with nucleotide
**[[1khb]] – EcPEPCK + GTP analog + Mg <br />
**[[1khe]] – EcPEPCK + GTP analog + Mn <br />
**[[2fah]] – cPEPCK + GDP + Mn <br />
**[[2qey]] – rPEPCK + GTP + Mn<br />
**[[5fh0]], [[5fh1]], [[5fh2]], [[5v97]] – rPEPCK (mutant) + Mn + GTP<br />
**[[4gnm]], [[4gnq]] - rPEPCK + oxalate + GTP + Mn<br />
**[[4gmw]], [[4gnl]], [[4gnp]] – rPEPCK + PEP + GDP + Mn <br />
**[[3dt2]], [[3dt4]], [[4gmu]] – rPEPCK + GTP + oxalate + Mn<br />
**[[3mof]], [[5fh3]], [[5v9g]] – rPEPCK (mutant) + GTP + oxalate + Mn<br />
**[[3dt7]], [[4gmm]], [[4gmz]], [[4gno]] – rPEPCK + GTP + sulfopyruvate + Mn<br />
**[[3moe]], [[4ox2]], [[5fh4]], [[5v9f]] – rPEPCK (mutant) + GTP + sulfopyruvate + Mn<br />
**[[3dtb]] – rPEPCK + GTP + phosphoglycolate + Mn<br />
**[[3moh]], [[5fh5]], [[5v9h]] – rPEPCK (mutant) + GDP + phosphoglycolate + Mn<br />
**[[2qf2]] – rPEPCK + GDP + oxaloacetate + Mn<br />
**[[4yw9]] – rPEPCK + inhibitor + Mn + GTP<br />
**[[4rcg]] – MtPEPCK + GDP + Mg <br />
**[[4r43]] – MtPEPCK + GDP + Mn <br />
**[[5i67]] – MtPEPCK (mutant) + Mn + GDP<br />
**[[4wl8]] – MtPEPCK + Mn + GTP analog<br />
**[[4wou]] – MtPEPCK + Mn + Zn + GDP<br />
**[[4wpu]] – MtPEPCK (mutant) + PEP + GDP <br />
*PEPCK


**[[2zci]] – PEPCK – ''Corynebacterium glutamicum'' <br />
**[[1ygg]] – AsPEPCK – ''Actinobacillus succinogenes''<br />
**[[1ylh]] – AsPEPCK + pyruvate + Mn<br />
**[[1ii2]] – PEPCK – ''Trypanosoma cruzi''<br />
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 11:39, 10 January 2023


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.

See also: Gluconeogenesis.

Structural highlights

E. coli GTP-driven PEPCK is located in a pocket at the enzyme surface[2]. Water molecules are shown as red spheres.

  • .
  • .

3D Structures of PEPCK

Phosphoenolpyruvate carboxykinase 3D structures


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

Drag the structure with the mouse to rotate

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

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

Michal Harel, Jaime Prilusky, Alexander Berchansky, Joel L. Sussman
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