Abstract: The present invention relates to biocatalysts catalyzing the formation of ?-olefins. In particular, the invention provides polypeptides with improved decarboxylase activity on C10-C16 free fatty acids, more particularly on C10 or C12 free fatty acids, as compared to the P450 fatty acid decarboxylase isolated from the Staphylococcus massiliensis strain S46 (Sm46). The invention further provides recombinant nucleic acids and vectors comprising the coding sequences encoding these polypeptides, genetically engineered host cells expressing said polypeptides and methods for the production of C9-C15 ?-olefins, more particularly C9 or C11 ?-olefins, using said polypeptides or said host cells.

Abstract: The present invention relates to the biosynthesis of ?-olefins. In particular, the invention provides methods for the production of medium-chain ?-olefins, more particularly C11 ?-olefins, using a polypeptide with decarboxylase activity on free fatty acids with 8 to 14 carbons, in particular on C8-C12 free fatty acids, more particularly on C12 free fatty acids, or a genetically engineered host cell expressing or overexpressing said polypeptide.

Abstract: The present invention relates to the biosynthesis of ?-olefins. In particular, the invention provides methods for the production of medium-chain ?-olefins, more particularly C11 ?-olefins, using a polypeptide with decarboxylase activity on free fatty acids with 8 to 14 carbons, in particular on C8-C12 free fatty acids, more particularly on C12 free fatty acids, or a genetically engineered host cell expressing or overexpressing said polypeptide.

Abstract: The biosynthesis of fungal bicyclo[2.2.2]diazaoctane indole alkaloids with a wide spectrum of biological activities have attracted increasing interest. Their intriguing mode of assembly has long been proposed to feature a non-ribosomal peptide synthetase, a presumed intramolecular Diels-Alderase, a variant number of prenyltransferases, and a series of oxidases responsible for the diverse tailoring modifications of their cyclodipeptide-based structural core. Until recently, the details of these biosynthetic pathways have remained largely unknown due to lack of information on the fungal derived biosynthetic gene clusters. Herein, we report a comparative analysis of four natural product metabolic systems of a select group of bicyclo[2.2.2]diazaoctane indole alkaloids including (+)/(?)-notoamide, paraherquamide and malbrancheamide, in which we propose an enzyme for each step in the biosynthetic pathway based on deep annotation and on-going biochemical studies.

Abstract: The biosynthesis of fungal bicyclo[2.2.2]diazaoctane indole alkaloids with a wide spectrum of biological activities have attracted increasing interest. Their intriguing mode of assembly has long been proposed to feature a non-ribosomal peptide synthetase, a presumed intramolecular Diels-Alderase, a variant number of prenyltransferases, and a series of oxidases responsible for the diverse tailoring modifications of their cyclodipeptide-based structural core. Until recently, the details of these biosynthetic pathways have remained largely unknown due to lack of information on the fungal derived biosynthetic gene clusters. Herein, we report a comparative analysis of four natural product metabolic systems of a select group of bicyclo[2.2.2]diazaoctane indole alkaloids including (+)/(?)-notoamide, paraherquamide and malbrancheamide, in which we propose an enzyme for each step in the biosynthetic pathway based on deep annotation and on-going biochemical studies.

Abstract: The present invention provides regio- and stereoselective oxidation of unactivated C—H bonds using an engineered mutant cytochrome P450 monooxygenase and an engineered substrate.

Abstract: The present invention provides chimeric cytochrome P450 enzymes fused to heterologous reductase domains to generate single-component, self-sufficient, more cost-effective and catalytically more active biosynthetic P450 monooxygenases.