Niehaus Lab
Principal Investigator: Thomas D Niehaus
Institution: University of Minnesota (Minneapolis, MN)
Primary Subfield: Molecular & Cell Bio
Recruitment Status: Inquire for rotation/fellowship opportunities
Research Focus
PROJECT SUMARY / ABSTRACT In general, enzymes are very precise at catalyzing a specific canonical reaction that fits within a particular metabolic network. Still, no enzyme is a perfect catalyst. The inherent flexibility of proteins makes it difficult for enzymes to distinguish their canonical substrate from structurally related compounds. Thus, many enzymes act on unintended substrates (i.e., substrate promiscuity). Substrate promiscuities result in the formation of unintended or damaged metabolites (i.e., metabolite damage) that can be a useless drain on metabolism, and may be inhibitory and/or reactive, sometimes leading to toxicity. Accordingly, metabolite damage repair enzymes exist for the specific purpose of counteracting metabolite damage, often by converting a damaged metabolite to a canonical one. The physiological importance of metabolite damage and its repair has been revealed over the past ~15 years as a handful of metabolic diseases in humans were discovered to be caused by disruption of metabolite damage repair genes, many of which are highly conserved across the three domains of life. The proposed project will address metabolite damage repair associated to the TCA c…
Active NIH Awards
- 5R35GM154803-03: Unraveling the physiological and metabolic impacts of a universal metabolite repair enzyme that removes a strong inhibitor of the TCA cycle (2026)
- 5R35GM154803-02: Unraveling the physiological and metabolic impacts of a universal metabolite repair enzyme that removes a strong inhibitor of the TCA cycle (2025)
- 1R35GM154803-01: Unraveling the physiological and metabolic impacts of a universal metabolite repair enzyme that removes a strong inhibitor of the TCA cycle (2024)
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