Indole-3-glycerol phosphate synthase (IGPS) catalyzes the indole-forming reaction in the bacterial tryptophan biosynthetic pathway. This pathway appears to be necessary for bacterial growth and may be a target for potential new anti-infective agents. In order to explore this possibility, more detailed information about IGPS enzyme-substrate interactions and its catalytic mechanism is required. We will present our latest results aimed at obtaining this data utilizing a combination of mutant M. tuberculosis IGPS proteins and substrate analogs. Conclusions regarding the roles of key protein residues and substrate functional groups will be presented.

<i>M. tuberculosis</i> IGP synthase: Substrate structure-function relationships and characterization of catalytically important residues

ACS Fall 2021

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M. tuberculosis IGP synthase: Substrate structure-function relationships and characterization of catalytically important residues