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Our efforts focus on developing a detailed understanding of the mechanisms by which enzymes catalyze biological reactions. Insights obtained from studies on enzyme mechanism can lead to the production of bio-active compounds and to the design of efficient synthetic catalysts.
Stereochemical control is a key component in the biosynthesis and metabolism of many biological compounds. As a result, many racemases and epimerases have evolved that catalyze the inversion of configuration about carbon. Most of these enzymes act at centers which are activated by an adjacent carbonyl functionality, and they abstract a relatively acidic proton. Our interests lie in studying enzymes that act on unactivated stereocenters and must employ unique reaction mechanisms. One example is ADP-heptose 6-epimerase that generates a key building block in bacterial lipopolysaccharide biosynthesis.
Stereochemical control is a key component in the biosynthesis and metabolism of many biological compounds. As a result, many racemases and epimerases have evolved that catalyze the inversion of configuration about carbon. Most of these enzymes act at centers which are activated by an adjacent carbonyl functionality, and they abstract a relatively acidic proton. Our interests lie in studying enzymes that act on unactivated stereocenters and must employ unique reaction mechanisms. One example is ADP-heptose 6-epimerase that generates a key building block in bacterial lipopolysaccharide biosynthesis.
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SSRN Electronic Journal (2022): 128971-128971
Kishore K. Mahalingan, E. Keith Keenan,Madeleine Strickland,Yan Li,Yanjie Liu, Haydn L. Ball,Martin E. Tanner,Nico Tjandra,Antonina Roll-Mecak
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