Fructose Bisphosphate Aldolase
From Proteopedia
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'''Fructose biphosphate aldolase''' | '''Fructose biphosphate aldolase''' | ||
| - | <scene name='Austin_Drake_Sandbox/Tetramer/3'>Fructose biphosphate aldolase</scene><ref name="jmol">Jmol: an open-source Java viewer for chemical structures in 3D. http://www.jmol.org/</ref> 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_w_water/3'>Catalytic Site Closeup</scene><ref name="jmol" /> 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.<ref>Voet, D, Voet, J, & Pratt, C. (2008). Fundamentals of biochemistry, third edition. Hoboken, NJ: Wiley & Sons, Inc.</ref> The enzyme is an a/B protein. It is part of the aldolase superfamily and the class I aldoses<ref>Protein: fructose-1,6-bisphosphate aldolase from human (homo sapiens), muscle isozyme. (2009). Retrieved from http://scop.mrc-lmb.cam.ac.uk</ref><scene name='Austin_Drake_Sandbox/Different_colors/1'>a Helices and B sheets</scene> can be seen in their specific regions concentrically located around the active site. | + | <scene name='Austin_Drake_Sandbox/Tetramer/3'>Fructose biphosphate aldolase</scene><ref name="jmol">Jmol: an open-source Java viewer for chemical structures in 3D. http://www.jmol.org/</ref> 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_w_water/3'>Catalytic Site Closeup</scene><ref name="jmol" /> 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.<ref>Voet, D, Voet, J, & Pratt, C. (2008). Fundamentals of biochemistry, third edition. Hoboken, NJ: Wiley & Sons, Inc.</ref> The enzyme is an a/B protein. It is part of the aldolase superfamily and the class I aldoses<ref>Protein: fructose-1,6-bisphosphate aldolase from human (homo sapiens), muscle isozyme. (2009). Retrieved from http://scop.mrc-lmb.cam.ac.uk</ref><scene name='Austin_Drake_Sandbox/Different_colors/1'>. a Helices and B sheets</scene><ref name="jmol" /> can be seen in their specific regions concentrically located around the active site. <scene name='Austin_Drake_Sandbox/B_sheet_barrel/2'>FBP is catalyzed inside the barrel.</scene><ref name="jmol" /> |
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| - | <scene name='Austin_Drake_Sandbox/B_sheet_barrel/2'>FBP | + | |
{{STRUCTURE_2ald | PDB=2ald | SCENE= }} | {{STRUCTURE_2ald | PDB=2ald | SCENE= }} | ||
<references/> | <references/> | ||
Revision as of 23:55, 28 February 2010
Fructose biphosphate aldolase
[1] 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. [1] 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.[2] The enzyme is an a/B protein. It is part of the aldolase superfamily and the class I aldoses[3][1] can be seen in their specific regions concentrically located around the active site. [1] Template:STRUCTURE 2ald
- ↑ 1.0 1.1 1.2 1.3 Jmol: an open-source Java viewer for chemical structures in 3D. http://www.jmol.org/
- ↑ Voet, D, Voet, J, & Pratt, C. (2008). Fundamentals of biochemistry, third edition. Hoboken, NJ: Wiley & Sons, Inc.
- ↑ Protein: fructose-1,6-bisphosphate aldolase from human (homo sapiens), muscle isozyme. (2009). Retrieved from http://scop.mrc-lmb.cam.ac.uk
Proteopedia Page Contributors and Editors (what is this?)
Austin Drake, David Canner, Jacob Holt, Alexander Berchansky, Michal Harel
