Raushel, Frank individual record
Distinguished Professor
Positions:
overview

Enzymes catalyze a remarkable variety of chemical reactions with extremely high rate enhancements and very selective substrate specificity. The research efforts in our laboratory are directed towards a more complete understanding of the fundamental principles involved in enzyme-catalyzed chemistry and the dependence on protein structure. The pursuit of this information will provide the framework for the rational and combinatorial redesign of these complex molecules in an effort to exploit and develop the properties of enzyme active sites for a variety of chemical, biological, and medicinal uses. The techniques that we are using to solve these problems include steady-state and stopped-flow kinetics, NMR and EPR spectroscopy, X-ray crystallography, and the synthesis of inhibitors and suicide substrates. We are also using recombinant DNA methods to construct new proteins with novel catalytic properties. These efforts are currently being directed to the reactions catalyzed by phosphotriesterase and enzymes involves in the degradation of lignin and the metabolism of novel carbohydrates from the human gut microbiome.



The phosphotriesterase enzyme catalyzes the hydrolysis of organophosphate insecticides and other toxic organophosphate nerve agents. We have discovered that the active site of this protein consists of a unique binuclear metal center for the activation of water. We are now investigating the structure and properties of this metal center as a model system for the evolution of enzyme structure and function. Toward this end we have mutated the active site of this enzyme in a research project to create novel enzymes with the ability to detect, destroy, and detoxify various chemical warfare agents such as sarin, soman, and VX. The Raushel laboratory is also engaged in a large scale research project that is focused on the development of novel strategies for the discovery of new enzymes.

selected publications
Academic Articles344
  • Riegert, A. S., Narindoshvili, T., Coricello, A., Richards, N., & Raushel, F. M. (2022). Correction to “Functional Characterization of Two PLP-Dependent Enzymes Involved in Capsular Polysaccharide Biosynthesis from Campylobacter jejuni”. Biochemistry. 61(1), 46-46.
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  • Riegert, A. S., Narindoshvili, T., Coricello, A., Richards, N., & Raushel, F. M. (2021). Functional Characterization of Two PLP-Dependent Enzymes Involved in Capsular Polysaccharide Biosynthesis from Campylobacter jejuni. Biochemistry. 60(37), 2836-2843.
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  • Bigley, A. N., Harvey, S. P., Narindoshvili, T., & Raushel, F. M. (2021). Substrate Analogues for the Enzyme-Catalyzed Detoxification of the Organophosphate Nerve Agents—Sarin, Soman, and Cyclosarin. Biochemistry. 60(38), 2875-2887.
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  • Holden, H. M., & Raushel, F. M. (2021). From the Three-Dimensional Structure of Phosphotriesterase.. Biochemistry. 60(46), 3413-3415.
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Conference Papers66
  • Yang, K., Ren, Z., Raushel, F. M., & Zhang, J. (2016). Structures of the Carbon-Phosphorus Lyase Complex Reveal the Binding Mode of the NBD-Like PhnK. Biophysical Journal. 110(3), 159a-159a.
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  • Hobbs, M. E., Williams, H. J., & Raushel, F. M. (2012). Discovery of an L-fucono-1,5-lactonase within cog3618 from the amidohydrolase superfamily. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY. 244,
  • Ornelas, A., Narindoshvili, T., Sugadev, R., Kumaran, D., Swaminathan, S., & Raushel, F. M. (2011). Characterization of members of the amidohydrolase superfamily in COG3964: Determining function of Atu3266 and Ef0837. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY. 242,
  • Goble, A. M., Zhang, Z., Swaminathan, S., & Raushel, F. M. (2011). Identification and structure determination of novel substituted purine deaminase enzymes. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY. 242,
  • Lund, L., Williams, H. J., & Raushel, F. M. (2010). Evidence for the utilization of formate as a substrate by carbamoyl phosphate synthetase. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY. 240,
patents
Patents2
chaired theses and dissertations
Email
raushel@tamu.edu
First Name
Frank
Last Name
Raushel
mailing address
Texas A&M University; Chemistry Department; 3255 TAMU
College Station, TX 77843-3255
USA