Directed evolution of microbial oxidative enzymes.
In the past year, a number of oxidative enzymes have been the target of directed evolution. Catalase reaction specificity has been shifted to peroxidase, the high pH, thermal and oxidative stability of a fungal peroxidase has been dramatically improved, and the substrate specificity of cytochrome P450 has been altered to include substrates that the wild-type enzymes are incapable of oxidizing.
Cherry
J R
JR
Product Improvement Group, Novo Nordisk Biotech, Inc., Davis, CA 95616, USA. cherry@nnbt.com
D001709:Biotechnology; D019475:Camphor 5-Monooxygenase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D002374:Catalase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D019020:Directed Molecular Evolution; D008829:Microbiology; D010088:Oxidoreductases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D009195:Peroxidase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity
D010088:Oxidoreductases; D002374:Catalase; D009195:Peroxidase; D019475:Camphor 5-Monooxygenase