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Whitman, Christian P., Ph.D. |
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Research Interests
My laboratory is interested in how enzymes evolve and how they work. We are studying two groups of enzymes, the tautomerase superfamily and the fumaryl acetoacetate hydrolase (FAH) superfamily. Both superfamilies likely evolved from common ancestors through divergent evolution. The members of the tautomerase superfamily use a conserved amino-terminal proline and an arginine to catalyze diverse reactions including tautomerization, dehalogenation, hydration, and decarboxylation. The FAH superfamily members use an enzyme-bound metal ion to catalyze hydrolysis, decarboxylation, and perhaps hydration reactions. Using a variety of mechanistic and structural techniques, we examine a range of reactions in these two groups so we can understand the principles used by nature to make new enzymes from old ones. Understanding this process will enable us to design novel biocatalysts through rational design or directed evolution. This knowledge also has implications for the evolution of enzymes that degrade antibiotics (leading to antibiotic-resistant bacteria) and environmental pollutants.
More information about Dr. Whitman > Enzyme Images > Publications | |
Division Information
Mailing Address:
The University of Texas
at Austin
Medicinal Chemistry
BME 6.202
College of Pharmacy
1 University Station,
C0850
Austin, TX
78712-0120
USA
Email Address: pharmacy
@www.utexas.edu
Phone:
Texas Enzyme Mechanisms Conference - Jan 8-9, 2010

Dr. Patrick Davis attended the University of Texas System
Leadership Institute's inaugural program, Leadership Dimensions I.
>Read more about the program.