Indole-3-glycerol phosphate synthase (IGPS) catalyzes the indole-forming reaction in the multi-step bacterial tryptophan biosynthetic pathway. This pathway appears to be necessary for bacterial growth and it could represent a target for potential new anti-infective agents in the future. In order to realize this possibility, more detailed information about IGPS enzyme-substrate interactions and its catalytic mechanism would be valuable. We will present our latest progress in characterizing specific enzyme-substrate and catalytic structure-function relationships in IGPS from <i>M. tuberculosis</i>. This work involves data obtained using both novel CdRP substrate analogs and mutant IGPS proteins. Conclusions regarding key protein residues and substrate functional groups will be included.

Structure-function relationships in substrate binding and catalysis in IGPS from <i>M. tuberculosis</i>

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

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Structure-function relationships in substrate binding and catalysis in IGPS from M. tuberculosis