title: Diversity of P450 enzymes in the biosynthesis of natural products.
abstract: Diverse oxygenation patterns of natural products generated by secondary metabolic pathways in microorganisms and plants are largely achieved through the tailoring reactions catalysed by cytochrome P450 enzymes (P450s). P450s are a large family of oxidative hemoproteins found in all life forms from prokaryotes to humans. Understanding the reactivity and selectivity of these fascinating C-H bond-activating catalysts will advance their use in generating valuable pharmaceuticals and products for medicine, agriculture and industry. A major strength of this P450 group is its set of established enzyme-substrate relationships, the source of the most detailed knowledge on how P450 enzymes work. Engineering microbial-derived P450 enzymes to accommodate alternative substrates and add new functions continues to be an important near- and long-term practical goal driving the structural characterization of these molecules. Understanding the natural evolution of P450 structure-function should accelerate metabolic engineering and directed evolutionary approaches to enhance diversification of natural product structures and other biosynthetic applications.
authors: Department of Pathology, Molecular Structure Group and Center for Discovery and Innovation in Parasitic Diseases (CDIPD), University of California San Francisco, San Francisco, California 94158, USA. larissa.podust@ucsf.edu
authors: Larissa M
authors: LM
authors: Podust
authors: David H
authors: DH
authors: Sherman
mesh_terms: D001688:Biological Products / Q000737:chemistry / Q000378:metabolism*; D002384:Catalysis; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry / Q000378:metabolism*; D005658:Fungi / Q000201:enzymology; D006801:Humans; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010944:Plants / Q000201:enzymology
chemical_list: D001688:Biological Products; D003577:Cytochrome P-450 Enzyme System