The disclosure relates to the field of fusion proteins. In some aspects, the disclosure relates to artificial fusion proteins comprising cytochrome P450 enzymes linked to reductase enzymes and uses thereof. In some aspects, the disclosure relates to corn-pounds produced by artificial cytochrome P450 enzymes.

The present invention relates to genetically modified enzymes obtained by rational design of the active site binding pocket of the prototypic enzyme 4-hydroxyphenylacetate 3-hydroxylase (4HPA3H) for hydroxylating a 4-hydroxyphenyl compound to yield a 3,4-dihydroxyphenyl compound and to biotechnological methods including in vivo and in vitro methods using said enzymes or catalytically active fragments thereof. Further provided is a method either using a suitable oxidase or hydroxylase further enabling the subsequent site specific methylation of the 3,4-dihydroxyphenyl compound in a coupled enzymatic reaction by providing a suitable O-methyltransferase. Finally, compositions obtainable by the aforementioned methods are disclosed.

As described herein, a hybrid voltage sensor genetically-encoded voltage indicator (GEVI) for mitochondria or endoplasmic reticulum includes a transmembrane domain, and a fluorescent protein, wherein a terminus of the transmembrane domain and a terminus of the fluorescent protein are covalently linked directly or by a linker comprising 1 to 20 amino acids, and wherein the transmembrane domain comprises SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4 or a peptide with greater than 85%, 90%, 95% or 98% identity to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 4. Also described are expression vectors, expression cassettes, and organelle membranes, as well as methods of determining the voltage across an organelle using the GEVIs.

Consumer product compositions having P450 fatty acid decarboxylases and methods of using said consumer products to provide a benefit by converting long chain fatty acids present in soils into terminal olefins.

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.

A detergent composition, preferably a manual dishwashing detergent composition, including one or more diol synthases capable of converting one or more unsaturated fatty acids into one or more oxylipins, and a surfactant system including one or more anionic surfactants and one or more co-surfactants selected from the group consisting of amphoteric surfactant, zwitterionic surfactant, and mixtures thereof. Method of using the detergent composition including a surfactant system and the diol synthases are also provided.

7-hydroxylation systems are provided, as well as methods for producing ?P-hydroxy derivatives of lithocholic acid and 3-keto-lithocholic acid from such systems. Also provided are recombinant organisms useful for the production of such enzymatic systems, and to plasmids that encode for such enzymes.

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.

What is described herein refers to isolated nucleic acid fragments encoding an oxygenase subunit (StyA) and a reductase subunit (StyB), wherein the polypeptide encoded for by the nucleotide sequence for the oxygenase subunit (StyA) and the nucleotide sequence for the reductase subunit (StyB) have activity towards chiral arylsulfides.

Disclosed are methods and compositions which may be used in human cytochrome P450 (CYP450) enzyme phenotyping. The methods and compositions typically utilize substrate for CYP3A5 comprising eplerenone which may be administered orally to a subject. Subsequently, metabolites of eplereone may be detected in the subject's saliva as well as any non- metabolized eplerenone to calculate a metabolic ratio for CYP3A5 enzyme in order to generate a phenytopic CYP3A5 enzyme profile for the subject.