Fructose Bisphosphate Aldolase
From Proteopedia
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.
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
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