Professor of Microbiology John Cronan, Professor of Biochemistry John Gerlt and Professor of Chemistry Jonathan Sweedler, along with colleagues from two other institutions, teamed up to discover the role of an enzyme known as HpbD in its bacterial host, Pelagibaca bermudensis.

Professor of Microbiology John Cronan, Professor of Biochemistry John Gerlt and Professor of Chemistry Jonathan Sweedler, along with colleagues from two other institutions, teamed up to discover the role of an enzyme known as HpbD in its bacterial host, Pelagibaca bermudensis. “At present, the number of proteins in the protein-sequence database is approaching 42 million,” Gerlt said. “But no more than 50 percent of these proteins have reliable functions assigned to them.” This study aimed to understand the function of HpbD as well as its target molecular partners using computational and laboratory analyses. The new effort is part of the Enzyme Function Initiative (EFI) at the Institute for Genomic Biology. This initiative, funded by the National Institutes of General Medical Sciences and led by Gerlt, is designed to address “complex problems that are of central importance to biomedical science but are beyond the means of any one research group.” The EFI focuses on enzymes of bacterial origin. The findings appear in the journal Nature.

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