Abstract

PLP is a chromophoric cofactor required for catalytic activity by a wide variety of enzymes. While PLP enzymes are thermally activated in vivo, it has been reported that some PLP enzymes can be activated by UV light. One enzyme that uses PLP as a cofactor is apsartate aminotransferase (AAT). Previous studies with AAT suggest that the carbanionic quinonoid intermediate is photogenerated by UV laser excitation. AAT is central to nitrogen metabolism in all living systems and has a large body of literature. As such, it is a useful prototype for the fundamental studies on this class of enzymes which were previously conducted. In order to verify these experimental results, the computer program COPASI was used. Two models of AAT mechanisms were examined using COPASI one with the quinonoid intermediate on the productive path and one with the quinonoid off the productive path.

Mentor

Delmar Larsen

Lab site

Center for Biophotonics Science and Technology (CBST)

Funding Acknowledgement

This material is based upon work supported by the S.D. Bechtel, Jr. Foundation and by the National Science Foundation under Grant No. 0952013. Any opinions, findings, and conclusions or recommendations expressed in this material are those of the authors and do not necessarily reflect the views of the S.D. Bechtel, Jr. Foundation or the National Science Foundation.

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URL: http://digitalcommons.calpoly.edu/star/78

 

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