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Fructose-1,6-bisphosphate (FBP) aldolase (E.C. 4.1.2.13) catalyzes the reversible aldol condensation of dihydroxyacetonephosphate (DHAP) and glyceraldehyde-3-phosphate (G3P) in glycolysis, gluconeogenesis and the Calvin cycle. FBP aldolases are categorized into two groups based on different catalytic mechanisms. Notably, Class II aldolase does not exist in animals or plants, making this enzyme a potential drug target for pathogenic microbial organisms such as Mycobacterium tuberculosis. A chromogenic substrate was synthesized as a FBP mimic. The chromogenic substrate can be applied to a direct chromogenic assay for monitoring the activity of Class II FBP aldolases and also to evaluate any good inhibitor. In addition, our research group has found that a commercially available antidote for heavy metal poisoning, 2,3-dimercapto-1-propanesulfonic acid (DMPS) is a good competitive inhibitor of Class II FBP aldolase. In order to improve the binding affinity of this inhibitor in the enzyme active site, new molecules based on this compound were rationally designed using molecular modeling.
About the author
Clarence is a recent MBA grad from Ivey Business School at Western University and currently working as a Marketing Specialist in a top Canadian telecomm company. He has impacted key decisions and been a catalyst for change. He completed his M.Sc. in Chemistry and B.Sc. in Biochemistry at University of Waterloo in Canada. He's a proud father of two.
