Poster Presentation 1B-26

 

Thermostability of a Hybrid Cytochrome P450 Enzyme Generated from CYP101 and CYP119

 

 

Abhijeet P. Borole* and Choo Y. Hamilton

 

 

Life Sciences Division

 Oak Ridge National Laboratory

Bldg. 4505, MS 6226

 Oak Ridge, TN 37831-6226

Phone:  (865)576-7421

Fax:  (865)574-6442

E-mail:  borolea@ornl.gov

 

 

 

Cytochrome P450 is one of the most versatile enzymes for oxygen activation of hydrophobic molecules such as polyaromatic hydrocarbons and alkanes.  Industrial application of these enzymes has been limited by their low stability and requirement for a cofactor.  In an attempt to increase thermostability of these enzymes, we are studying shuffling and chimeragenesis with related thermostable enzymes. CYP101 is our model hydrocarbon oxidizing enzyme and CYP119 is the model thermostable enzyme.  Chimeras generated from these two proteins show retention of the temperature stability but alteration in substrate specificity.  Preliminary results from a combined rational design followed by random shuffling strategy to produce a functional thermostable protein will be discussed.