The disclosure relates to omega-hydroxylated fatty acid derivatives and methods of producing them. Herein, the disclosure encompasses a novel and environmentally friendly production method that provides omega-hydroxylated fatty acid derivatives at high purity and yield. Further encompassed are recombinant microorganisms that produce omega-hydroxylated fatty acid derivatives through selective fermentation.

Modified cells suitable for the production of ergot alkaloids include engineered recombinant cells having one or more genes that code for one or more enzymes in the biosynthetic pathway from tryptophan to D-lysergic acid (DLA). Methods of culturing the engineered recombinant cells can be used for the production of DLA and other ergot alkaloids.

The present invention provides improved P450-BM3 variants with improved activity. In some embodiments, the P450-BM3 variants exhibit improved activity over a wide range of substrates.

The present invention provides improved P450-BM3 variants with improved activity. In some embodiments, the P450-BM3 variants exhibit improved activity over a wide range of substrates.

The present invention provides improved P450-BM3 variants with improved activity. In some embodiments, the P450-BM3 variants exhibit improved activity over a wide range of substrates.

This invention relates to modified hydroxylases. The invention further relates to cells expressing such modified hydroxylases and methods of producing hydroxylated alkanes by contacting a suitable substrate with such cells.

The present invention provides improved P450-BM3 variants with improved activity. In some embodiments, the P450-BM3 variants exhibit improved activity over a wide range of substrates.

Provided is a recombinant microorganism including an exogenous gene encoding a bacterial cytochrome P450 protein or a variant thereof, a composition including the recombinant P450 protein or the variant thereof, which is used for removing CH.sub.nF.sub.4-n (n is an integer of 0 to 3) in a sample, and a method of reducing a concentration of CH.sub.nF.sub.4-n in the sample.

This disclosure provides a method of preparing a silanol-functional organosilicon compound with a cytochrome P450 variant that facilitates the oxidization of a silyl hydride group to a silanol group in the presence of oxygen. The method includes combining the cytochrome P450 variant and an organosilicon compound having at least one silicon-bonded hydrogen atom to give a reaction mixture and exposing the reaction mixture to oxygen to oxidize the organosilicon compound, thereby preparing the silanol-functional organosilicon compound. Cytochrome P450 variants suitable for use in the method are also disclosed, along with methods for engineering and optimizing the same. Nucleic acids encoding the cytochrome P450 variants and compositions, expression vectors, and host cells including the same are also disclosed.

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.