Phosphoenolpyruvate carboxylase: Difference between revisions

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Most proposed catalytic reaction mechanisms suggest that PEPC catalyzes an ordered multistep reaction in which the preferred order of reactant binding to the active site are: first the bivalent cation ( Mg2+ or Mn2+), then PEP and lastly bicarbonate (HCO3- ) <ref name="kai2003"/><ref name="Izui2004"/>. In a review article on the subject, Izui et al., 2004 <ref name="Izui2004"/>, proposes a detailed reaction mechanism for the enzyme, based on maize and'' E.coli'' PEPC structures in which PEP is located in a hydrophobic pocket consisting of W248, L504, and M538 residues. In this model, H177 is a critically important catalytic base as it is supposed to play a role in stabilizing the carboxyphosphate intermediate and abstracting a proton from its carboxyl group.
Most proposed catalytic reaction mechanisms suggest that PEPC catalyzes an ordered multistep reaction in which the preferred order of reactant binding to the active site are: first the bivalent cation ( Mg2+ or Mn2+), then PEP and lastly bicarbonate (HCO3- ) <ref name="kai2003"/><ref name="Izui2004"/>. In a review article on the subject, Izui et al., 2004 <ref name="Izui2004"/>, proposes a detailed reaction mechanism for the enzyme, based on maize and'' E.coli'' PEPC structures in which PEP is located in a hydrophobic pocket consisting of W248, L504, and M538 residues. In this model, H177 is a critically important catalytic base as it is supposed to play a role in stabilizing the carboxyphosphate intermediate and abstracting a proton from its carboxyl group.


[[Image:PEPC reaction mechanism.png|center|frame|caption position=bottom|'''Figure 5''' Catalytic mechanism of PEPC based on maize C4-PEPC and ''E. coli'' PEPC crystal structures and the three-step reaction model. The hydrophobic pocket is shown as yellow circles and the residues show maize numbering. Adapted from Izui et al. 2004. <ref name="Izui2004"/>]]
[[Image:PEPC reaction mechanism.png|center|thumb|600 px|caption position=bottom|'''Figure 5''' Catalytic mechanism of PEPC based on maize C4-PEPC and ''E. coli'' PEPC crystal structures and the three-step reaction model. The hydrophobic pocket is shown as yellow circles and the residues show maize numbering. Adapted from Izui et al. 2004. <ref name="Izui2004"/>]]


</StructureSection>
</StructureSection>

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