UMSI 2000 Annual Report: Mark Distefano, Principal Investigator Previous Page  |  Table of Contents  |  Next Page

Mark Distefano, Principal Investigator


Design of Semisynthetic Enzymes Based on Fatty Acid Binding Proteins

This work is developing enanatioselective catalysts that are based on protein cavities. This approach for catalyst design combines elements of host-guest chemistry with a highly flexible protein scaffold that can be manipulated by both chemical modification and recombinant DNA methods. The ability to prepare such catalysts could have a significant impact on the manufacture of a wide variety of specialty chemicals.

Research Group

Dietmar Haring, Research Associate
Tamara Kale, Graduate Student Researcher
Hao Kuang, Graduate Student Researcher
Evelyn Mayaan, Undergraduate Student Researcher
Dongfeng Qi, Graduate Student Researcher
Amy Tann, Graduate Student Researcher
Tammy Turek, Graduate Student Researcher

Specific aims of this work include improving the efficiency and controling the specificity of transaminating catalysts based on protein cavities using site directed mutagenesis, assessing whether changes in cofactor structure can be used to modulate the properties of transaminating catalysts based on protein cavities, and expanding the chemistry that can be performed using protein cavity based catalysts to include C-C bond formation. Computer modeling is being done at the Supercomputing Institute-Medicinal Chemistry Visualization/Workstation Laboratory.