This paper describes successful entrapment of previously uncharacterized reaction intermediate of MoaC reaction using an uncleavable substrate analog, 3′,8-cH2GTP. Intriguingly, the trapped intermediate was tightly bound to MoaC, likely through covalent modification, making the analog as the first mechanism-based inhibitor of bacterial Moco biosynthesis. The results revealed that the unique tetracyclic structure of cPMP (MoaC product) was constructed via a concerted formation of pterin and cyclic phosphate rings, which is distinct from previously proposed stepwise mechanism. Brad found the irreversible inhibition and performed most of the basic characterization, and Edward performed some nice follow up experiments including the MS characterization of the inhibited MoaC.
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- Bach received TriCEM fellowship to study the natural evolution of antibiotics
- Hai’s paper on the discovery of radical SAM oxygenase is published in JACS
- Elisha and Rachel presented posters at SURF
- Chitin synthase structure paper was published in Nature Structural & Molecular Biology
- Haoran successfully defended his Ph.D. dissertation
- Our latest manuscript about malayamycin biosynthesis was published in ACS Chemical Biology
- Haoran received 2021-2022 Chancellor’s Award for Research Excellence (CARE)
- Our perspective on MoaA and MoaC is published in ACS Bio Med Chem Au
- Haoran’s paper is highlighted in JACS Spotlight
- Haoran’s paper is published in JACS.
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