Ph.D., Molecular Biology, University of Pennsylvania SOM, 2003
B.S., Biology, Massachusetts Institute of Technology, 1986
The overall goal of my research is to provide a better understanding of energy metabolism in the pathogenic protist Entamoeba histolytica. This microbe is a scavenger that lacks ATP-generating mitochondria and hydrogenosomes as well as many common metabolic pathways. Thus, glycolysis is thought to be a primary pathway for ATP production. Glycolysis and the downstream conversion of pyruvate to acetyl-CoA and subsequently to acetate are atypical in several ways in E. histolytica. The glycolytic enzymes phosphofructokinase and pyruvate kinase are replaced by PPi-dependent phosphofructokinase and PPi-dependent pyruvate phosphate dikinase, and pyruvate:ferredoxin oxidoreductase replaces pyruvate dehydrogenase for conversion of pyruvate to acetyl-CoA. As acetyl-CoA cannot enter the citric acid cycle, ADP-forming acetyl-CoA synthetase (Ads) is present in E. histolytica to break down acetyl-CoA to generate additional ATP and recycle CoA. In addition, a PPi-forming acetate kinase (Ack) is present that may serve to supply PPi for glycolysis. My research focuses on the enzymology and physiological role of Ads and Ack.
T Taylor, C Ingram-Smith, and KS Smith. 2015. Biochemical and kinetic characterization of the eukaryotic phosphotransacetylase class IIa enzyme from Phytophthora ramorum. Eukaryotic Cell 14:652-660.
C Ingram-Smith*, J Wharton, C Reinholz, T Doucet, R Hesler, and KS Smith*. 2015. The role of active site residues in ATP binding and catalysis in the Methanosarcina thermophila acetate kinase. Life (Basel.) 5:861-871. (* co-corresponding authors)
C Jones and C Ingram-Smith. 2014. Biochemical and kinetic characterization of the recombinant ADP-forming acetyl-CoA synthetase from the amitochondriate protozoan Entamoeba histolytica. Eukaryotic Cell 13:1530-1537.
W Yang, C Catalanotti, S D’Adamo, TM Wittkopp, C Ingram-Smith, L Mackinder, TE Miller, AL Heuberger, G Peers, KS Smith, MC Jonikas, AR Grossman, and MC Posewitz. 2014. Alternative acetate production pathways in Chlamydomonas reinhardtii during dark anoxia and the dominant role of chloroplasts in fermentative acetate production. Plant Cell 26:4499-4518.
K Glenn, C Ingram-Smith, and KS Smith. 2014. Biochemical and kinetic characterization of xylulose 5-phosphate/fructose 6-phosphate phosphoketolase 2 (Xfp2) from Cryptococcus neoformans. Eukaryotic Cell 13:657-663.
TM Thaker, M Tanabe, M Fowler, AM Preininger, C Ingram-Smith, KS Smith, and TM Iverson. 2013. Crystal structures of acetate kinases from the eukaryotic pathogens Entamoeba histolytica and Cryptococcus neoformans. Journal of Structural Biology 181:185-189.