Dr. Frantom is an Associate Professor in the Department of Chemistry & Biochemistry. His lab has expertise in mechanistic enzymology, hydrogen/deuterium exchange mass spectrometry, and application of sequence similarity networks to enzyme superfamilies'. Overall research questions focus on characterizing structure/function relationships that govern enzyme function and regulation. Dr. Frantom’s lab is currently supported by funding from the NIH.
Representative Publications
- Biochemical characterization of 2-phosphinomethylmalate synthase from Streptomyces hygroscopicus: a member of the DRE-TIM metallolyase superfamily. J. V. Conte, P. A. Frantom Arch. Biochem. Biophys. 691: 108489, 2020.
- Structural evidence for dimer-interface-driven regulation of the type II cysteine desulfurase, SufS J. A. Dunkle, M. R. Bruno, F. W. Outten, P. A. Frantom. Biochemistry 58: 687-696, 2019.
- Distinct mechanisms of substrate selectivity in the DRE-TIM metallolyase superfamily: a role for the leuA dimer regulatory domain. W. Chen, P. A. Frantom Arch. Biochem. Biophys. 664: 1-8, 2019.
- Changes in protein dynamics in Escherichia coli SufS reveal a possible conserved regulatory mechanism in Type II cysteine desulfurase systems D. Kim, H. Singh, Y. Dai, G. Dong, L. S. Busenlehner, F. W. Outten, P. A. Frantom. Biochemistry, 57: 5210-5217, 2018.
- Improving functional annotation in the DRE-TIM metallolyase superfamily through identification of active site fingerprints. G. Kumar, J. L. Johnson, P. A. Frantom. Biochemistry 55: 1863-1872, 2016
Research Interests
Recent research in the Frantom laboratory focuses on characterizing the role of protein-protein interactions in bacterial iron-sulfur cluster bioassembly pathways. This work led to the identification of a conserved regulatory mechanism for type II cysteine desulfurase enzymes. Our group is also interested in mechanisms of glycosyltransferase enzymes, which play a key role in glycobiology. In a previous project, sequence similarity networks were used to identify mechanisms of functional and regulatory diversity in the DRE-TIM metallolyase superfamily.
