In Print: Tatyana Karabencheva-Christova Revealing the Catalytic Strategy of FTO

Diagram of the FTO enzyme catalysis
The FTO enzyme catalyzes the reaction of hydroxylation of 6-methyladenine (m6A) to 6-hydroxymethyl adenine (hm6-A) and then the reaction of oxidation of hm6-A to 6-formyl adenine (f6A). Mutations of the residues in the second coordination sphere influence the activation barrier of the Hydrogen Atom Transfer (HAT) which is the rate-limiting step.

A team from the Department of Chemistry led by Associate Professor Tatyana Karabencheva-Christova and including Ph.D. student Ann Varghese (first author); former Ph.D. students Sodiq Waheed ’23 (Ph.D. Computational Chemistry, currently a researcher at Lilly Corporate Center, Indianapolis) and Shobhit Chaturvedi ’22 (M.S. Ph.D. Chemistry, currently a postdoctoral researcher at UCLA); and undergraduate students Isabella DiCastri, Ciara LaRouche and Brendan Kaski has published an article in Chem Catalysis.

The article is titled “Revealing the catalytic strategy of FTO.” It provides unique insight into the catalytic mechanism of the fat-mass and obesity-associated protein (FTO), which is an Fe(II)- and 2-oxoglutarate (2OG)-dependent oxygenase targeted for treating obesity and cancer. The study reveals that the mutant R316Q, which is related to diseases, slows down the O2 activation and hydrogen atom transfer rates.

Professor Christo Christov (Chem) is a collaborator in this study, along with Nicolai Lehnert of the University of Michigan and Deyu Li of the University of Rhode Island.

The study is funded by the National Institutes of Health grant 2R15GM132873-02.

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