- Frank Raushel
- Professor of Chemistry and of Biochemistry and Biophysics
- ILSB Room 1214A
- Undergraduate Education
- B.A. St. Thomas College (1972)
- Graduate Education
- Ph.D. University of Wisconsin, Madison (1976)
- Postdoc. The Pennsylvania State University (1976-80)
- Joined Texas A&M in 1980
Mechanism and Evolution of Enzyme Active Sites
Enzymes catalyze a remarkable variety of chemical reactions with extremely high rate enhancements and very selective specificities. Our research is directed toward understanding enzyme-catalyzed chemistry and protein structure. Acquiring this information shall provide the framework for the redesign of these complex molecules in an effort to exploit the properties of enzyme active sites for a variety of chemical and medicinal uses. The techniques we use include steady-state and stopped-flow kinetics, NMR spectroscopy, x-ray crystallography, synthesis of inhibitors and suicide substrates, and site-directed mutagenesis to construct new proteins with altered properties. We are applying these methods to the reactions catalyzed by carbamoyl phosphate synthetase, phospho-triesterase, ribonuclease T1and kanamycin nucleotidyl transferase. Phosphotriesterase catalyzes the detoxification of organophosphate insecticides. We recently discovered that the active site consists of a unique binuclear metal center and are now investigating the structure and properties of this metal center as a tool for the evolution of enzyme structure and function. Carbamoyl phosphate synthetase catalyzes the formation of the key precursor for the biosynthesis of arginine and pyrimidine nucleotide. This complex heterodimeric protein contains unique binding sites for 10 substrates, allosteric ligands and metal ion activators.
Nemmara, VV, Xiang, DF, Fedorov, AA, Fedorov, EV, Bonanno, JB, Almo, SC et al.. Substrate Profile of the Phosphotriesterase Homology Protein from Escherichia coli. Biochemistry. 2018;57 (43):6219-6227.
Hogancamp, TN, Mabanglo, MF, Raushel, FM. Structure and Reaction Mechanism of the LigJ Hydratase: An Enzyme Critical for the Bacterial Degradation of Lignin in the Protocatechuate 4,5-Cleavage Pathway. Biochemistry. 2018;57 (40):5841-5850.
Halling, P, Fitzpatrick, PF, Raushel, FM, Rohwer, J, Schnell, S, Wittig, U et al.. An empirical analysis of enzyme function reporting for experimental reproducibility: Missing/incomplete information in published papers. Biophys. Chem. 2018;242 :22-27.
Ghodge, SV, Raushel, FM. Structure, Mechanism, and Substrate Profiles of the Trinuclear Metallophosphatases from the Amidohydrolase Superfamily. Meth. Enzymol. 2018;607 :187-216.
Taylor, ZW, Chamberlain, AR, Raushel, FM. Substrate Specificity and Chemical Mechanism for the Reaction Catalyzed by Glutamine Kinase. Biochemistry. 2018;57 (37):5447-5455.
Mukherjee, K, Narindoshvili, T, Raushel, FM. Discovery of a Kojibiose Phosphorylase in Escherichia coli K-12. Biochemistry. 2018;57 (19):2857-2867.
Hogancamp, TN, Raushel, FM. Functional Annotation of LigU as a 1,3-Allylic Isomerase during the Degradation of Lignin in the Protocatechuate 4,5-Cleavage Pathway from the Soil Bacterium Sphingobium sp. SYK-6. Biochemistry. 2018;57 (19):2837-2845.
Taylor, ZW, Raushel, FM. Cytidine Diphosphoramidate Kinase: An Enzyme Required for the Biosynthesis of the O-Methyl Phosphoramidate Modification in the Capsular Polysaccharides of Campylobacter jejuni. Biochemistry. 2018;57 (15):2238-2244.
Bigley, AN, Narindoshvili, T, Xiang, DF, Raushel, FM. Multiple Reaction Products from the Hydrolysis of Chiral and Prochiral Organophosphate Substrates by the Phosphotriesterase from Sphingobium sp. TCM1. Biochemistry. 2018;57 (12):1842-1846.
Bae, SY, Myslinski, JM, McMahon, LR, Height, JJ, Bigley, AN, Raushel, FM et al.. An OPAA enzyme mutant with increased catalytic efficiency on the nerve agents sarin, soman, and GP. Enzyme Microb. Technol. 2018;112 :65-71.