Fructose Bisphosphate Aldolase
From Proteopedia
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'''Introduction and Structure''' | '''Introduction and Structure''' | ||
| - | <scene name='Austin_Drake_Sandbox/Tetramer/3'>Fructose bisphosphate aldolase</scene> is an enzyme in glycolysis. It catalyzes the cleavage of fructose-1,6-bisphosphate into dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GAP). It can also catalyze the cleavage of fructose 1-phosphate to diydroxyacetone and glyceraldehyde. Different isozymes exhibit preferences for either or both of the substrates. | + | <scene name='Austin_Drake_Sandbox/Tetramer/3'>Fructose bisphosphate aldolase</scene> is an enzyme in glycolysis. It catalyzes the cleavage of fructose-1,6-bisphosphate into dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GAP). It can also catalyze the cleavage of fructose 1-phosphate to diydroxyacetone and glyceraldehyde. Different isozymes exhibit preferences for either or both of the substrates. It normally exists as a homotetramer. Each monomeric unit consists of eight alpha helices and eight beta sheets. |
The reaction is an aldol cleavage, or otherwise termed, retro aldo condensation. Catalysis occurs by the formation of a Schiff's 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 <scene name='Austin_Drake_Sandbox/Catalytic_site_w_water/3'>Asp33</scene>. Aldol cleavage produces GAP and an enamine precursor to DHAP. Tautomerization, protonation and the hydrolysis of the Schiff's 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/B_sheet_barrel/2'>FBP is catalyzed inside the barrel.</scene> | The reaction is an aldol cleavage, or otherwise termed, retro aldo condensation. Catalysis occurs by the formation of a Schiff's 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 <scene name='Austin_Drake_Sandbox/Catalytic_site_w_water/3'>Asp33</scene>. Aldol cleavage produces GAP and an enamine precursor to DHAP. Tautomerization, protonation and the hydrolysis of the Schiff's 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/B_sheet_barrel/2'>FBP is catalyzed inside the barrel.</scene> | ||
Revision as of 00:19, 18 March 2010
Fructose bisphosphate aldolase
Introduction and Structure
is an enzyme in glycolysis. It catalyzes the cleavage of fructose-1,6-bisphosphate into dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GAP). It can also catalyze the cleavage of fructose 1-phosphate to diydroxyacetone and glyceraldehyde. Different isozymes exhibit preferences for either or both of the substrates. It normally exists as a homotetramer. Each monomeric unit consists of eight alpha helices and eight beta sheets.
The reaction is an aldol cleavage, or otherwise termed, retro aldo condensation. Catalysis occurs by the formation of a Schiff's 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 . Aldol cleavage produces GAP and an enamine precursor to DHAP. Tautomerization, protonation and the hydrolysis of the Schiff's base produce the final product of DHAP and the active enzyme.[1] The enzyme is an a/B protein. It is part of the aldolase superfamily and the class I aldoses[2] can be seen in their specific regions concentrically located around the active site. Template:STRUCTURE 2ald
References
- ↑ 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
