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 P4...

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Veröffentlicht in:	Current Opinion in Biotechnology 2000-06, Vol.11 (3), p.250-254
1. Verfasser:	Cherry, Joel R
Format:	Artikel
Sprache:	eng
Schlagworte:	Biotechnology Camphor 5-Monooxygenase - chemistry Camphor 5-Monooxygenase - genetics Camphor 5-Monooxygenase - metabolism Catalase Catalase - chemistry Catalase - genetics Catalase - metabolism Cytochrome P450 Dioxygenase directed evolution Directed Molecular Evolution Microbiology Oxidoreductases - chemistry Oxidoreductases - genetics Oxidoreductases - metabolism Peroxidase Peroxidase - chemistry Peroxidase - genetics Peroxidase - metabolism Substrate Specificity
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Beschreibung
Zusammenfassung:	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.
ISSN:	0958-1669 1879-0429
DOI:	10.1016/S0958-1669(00)00092-6