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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.
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Biochemistryno. 5 (2024): 688-698
Manas K Ghosh,Tamari Narindoshvili,James B Thoden, Mitchell E Schumann,Hazel M Holden,Frank M Raushel
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Biochemistryno. 21 (2023): 3145-3158
Biochemistryno. 7 (2023): 1287-1297
Dat Truong,Andrew Mcmillan,Denis Odokonyero, Rebecca Skouby,Jamison Huddleston, Susan Fults, Reethu Bayana, Royer Murugarra,Mingzhao Zhu,Kenneth Hull,Daniel Romo,Frank Raushel,
PROTEIN SCIENCEno. 12 (2023)
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Biochemistryno. 20 (2023): 3012-3019
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