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News: Virtual Enzymes
Citation:
GLASER, J. A. News: Virtual Enzymes. 10.1007/s10098-008-0, CLEAN TECHNOLOGIES AND ENVIRONMENTAL POLICY. Springer-Verlag, New York, NY, 10(3):227-230, (2008).
Impact/Purpose:
publish information
Description:
In biochemical systems a host of “nature’s catalysts” conduct chemical transformations at physiological temperatures, high substrate conversion, high optical activity integrity, and single reactive center substrate changes. All of these traits are highly esteemed in the pursuit of “green” chemical synthetic technology for fine chemicals and pharmaceuticals. Researchers have recently reported the ability to use of computer design approaches to eliciting the active site architecture and the synthesis of 72 candidate retro-aldol enzymes from a field of more than 180,000. The Rosetta protein structure program was employed to generate the field of potential enzyme structures. The structures of synthesized enzymes were confirmed by X-ray crystallography. Thirty-two of the synthesized enzymes showed desired enzymatic activity with a range of catalytic activities. Despite this success, the catalytic activities of the synthesized enzymes were less that 100,000 times as active as comparable naturally occurring enzymes. However, the synthetic enzymes were shown to have activity to non-naturally occurring substrates such as 4-hydroxy-4-(6-methoxy-2-naphthyl)-1-butanone. This activity is promising for the enzymatic conversion of synthetic intermediates used to construct fine chemicals and pharmaceutical.
