Fructose Bisphosphate Aldolase: Difference between revisions
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Revision as of 23:38, 1 March 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
References
- ↑ 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