Fructose Bisphosphate Aldolase: Difference between revisions

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Fructose biphosphate aldolase is an enzyme in glycolysis.  It catalyzes the breakdown of fructose-1,6-biophosphate into dihydroxyacetone phosphate (DHAP) and glyceraldehyde-2-phosphate (GAP).  The reaction is an aldol cleavage, or otherwise termed, retro aldo condensation.  Catalysis occurs by the formation of a Schiff base (an imine resulting from a ketone and amine) from the amine of the aldolase's Lys229 and the open-ring form of FBP accompanied by stabilization from Asp33.  <scene name='Austin_Drake_Sandbox/Catalytic_site/1'>Catalytic Site</scene> aldol cleavage produces GAP and an enamine precursor to DHAP.  Tautomerization, protonation and the hydrolysis of the Schiff base produce the final product of DHAP and the active enzyme.
Fructose biphosphate aldolase is an enzyme in glycolysis.  It catalyzes the breakdown of fructose-1,6-biophosphate into dihydroxyacetone phosphate (DHAP) and glyceraldehyde-2-phosphate (GAP).  The reaction is an aldol cleavage, or otherwise termed, retro aldo condensation.  Catalysis occurs by the formation of a Schiff base (an imine resulting from a ketone and amine) from the amine of the aldolase's Lys229 and the open-ring form of FBP accompanied by stabilization from Asp33.  <scene name='Austin_Drake_Sandbox/Catalytic_site/1'>Catalytic Site</scene> aldol cleavage produces GAP and an enamine precursor to DHAP.  Tautomerization, protonation and the hydrolysis of the Schiff base produce the final product of DHAP and the active enzyme.


<scene name='Austin_Drake_Sandbox/B_sheet_barrel/2'>TextToBeDisplayed</scene>
<scene name='Austin_Drake_Sandbox/B_sheet_barrel/2'>FBP fits here</scene>
{{STRUCTURE_2ald |  PDB=2ald  |  SCENE=  }}
{{STRUCTURE_2ald |  PDB=2ald  |  SCENE=  }}




Jmol: an open-source Java viewer for chemical structures in 3D. http://www.jmol.org/
Jmol: an open-source Java viewer for chemical structures in 3D. http://www.jmol.org/

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

Austin Drake, David Canner, Michal Harel, Alexander Berchansky, Jacob Holt