Abstract: Described herein is a method of producing a drimane sesquiterpene such as albicanol, drimenol and/or derivatives thereof by contacting at least one polypeptide with farnesyl diphosphate (FPP) with a polypeptide including a Haloacid dehalogenase (HAD)-like hydrolase domain and having bifunctional terpene synthase activity. The method may be performed in vitro or in vivo. Also described herein are amino acid sequences of polypeptides useful in the methods and nucleic acids encoding the polypeptides described. The described method further provides host cells or organisms genetically modified to express the polypeptides and useful to produce a drimane sesquiterpene such as albicanol, drimenol and/or derivatives thereof.

Abstract: Described herein are biocatalytic methods of producing terpene degradation products useful as starting material for the production of perfumery ingredients, such as, for example, ambrox. In particular novel terpene degrading polypeptides (enal-cleaving polypeptides) and novel peptides converting terpenes compounds to oxygenated derivatives (oxygenases) and mutants and variants derived therefrom are described which may be applied in novel types of fully enzymatic multistep degradation pathways allowing the controlled, stepwise conversion and degradation of linear or cyclic terpene substrates. Said novel biosynthetic strategies allow the fully biochemical synthesis of valuable terpene-derived compounds, like for example manooloxy or gamma ambrol. Also described herein are recombinant host organisms carrying the required set of genetic information for the functional expression of the set of enzymes necessary for catalyzing the combination of enzymatic conversion and degradation steps.

Abstract: Described herein is a method of producing a drimane sesquiterpene such as albicanol, drimenol and/or derivatives thereof by contacting at least one polypeptide with farnesyl diphosphate (FPP) with a polypeptide including a Haloacid dehalogenase (HAD)-like hydrolase domain and having bifunctional terpene synthase activity. The method may be performed in vitro or in vivo. Also described herein are amino acid sequences of polypeptides useful in the methods and nucleic acids encoding the polypeptides described. The described method further provides host cells or organisms genetically modified to express the polypeptides and useful to produce a drimane sesquiterpene such as albicanol, drimenol and/or derivatives thereof.

Abstract: Described herein is a method of producing a drimane sesquiterpene such as albicanol, drimenol and/or derivatives thereof by contacting at least one polypeptide with farnesyl diphosphate (FPP) with a polypeptide including a Haloacid dehalogenase (HAD)-like hydrolase domain and having bifunctional terpene synthase activity. The method may be performed in vitro or in vivo. Also described herein are amino acid sequences of polypeptides useful in the methods and nucleic acids encoding the polypeptides described. The described method further provides host cells or organisms genetically modified to express the polypeptides and useful to produce a drimane sesquiterpene such as albicanol, drimenol and/or derivatives thereof.

Abstract: Described herein is a method of producing a drimane sesquiterpene such as albicanol, drimenol and/or derivatives thereof by contacting at least one polypeptide with farnesyl diphosphate (FPP) with a polypeptide comprising a Haloacid dehalogenase (HAD)-like hydrolase domain and having bifunctional terpene synthase activity. The method may be performed in vitro or in vivo. Also described herein are amino acid sequences of polypeptides useful in the methods and nucleic acids encoding the polypeptides described. The described method further provides host cells or organisms genetically modified to express the polypeptides and useful to produce a drimane sesquiterpene such as albicanol, drimenol and/or derivatives thereof.

Abstract: Provided herein are biocatalytic methods of producing terpene compounds by applying a novel type of phosphatase enzyme. The method allows the fully biochemical synthesis of terpene compounds, like for example copalol and labdendiol, and derivatives thereof, which serve as valuable intermediates for the production of perfumery ingredients, such as, for example, ambrox. Also provided are novel fully biochemical multistep processes for the production of such compounds as well as novel phosphatase enzymes and mutants and variants derived therefrom.

Abstract: Described herein are novel methods for the acetyl transferase-catalyzed production of drimanyl-acetate compounds by the acetylation of the respective drimanyl alcohol sources performed in vitro or in vivo. Also described herein is the identification of enzymes having corresponding acetyl transferase activity from different microbial and plant sources. Also described herein is the provision of enzyme mutants derived from the newly identified enzymes. Further described herein is the provision of corresponding coding sequences of such enzymes and mutants, recombinant vectors, and recombinant host cells suitable for the production of such acetyl transferases and mutants and for performing the novel production methods of drimanyl acetate compounds. Still further described herein is a method of using such drimanyl acetates as intermediates for the production of odorant, flavor or fragrance or insect/pest control ingredients.

Abstract: Provided herein are biocatalytic methods of producing terpene compounds by applying a novel type of phosphatase enzyme. The method allows the fully biochemical synthesis of terpene compounds, like for example copalol and labdendiol, and derivatives thereof, which serve as valuable intermediates for the production of perfumery ingredients, such as, for example, ambrox. Also provided are novel fully biochemical multistep processes for the production of such compounds as well as novel phosphatase enzymes and mutants and variants derived therefrom.

Abstract: Described herein are methods of producing (+)-manool, the methods including: contacting geranylgeranyl diphosphate with a copalyl diphosphate (CPP) synthase to form a (9S, 10S)-copalyl diphosphate and contacting the CPP with a sclareol synthase enzyme to form (+)-manool and derivatives thereof. Also described herein are nucleic acids encoding CPP synthases and sclareol synthases for use in the methods. Further described herein are expression vectors and non-human host organisms and cells including nucleic acids encoding a CPP synthase and a sclareol synthase as described herein.

Abstract: Described herein are methods of producing (+)-manool, the methods including: contacting geranylgeranyl diphosphate with a copalyl diphosphate (CPP) synthase to form a (9S, 10S)-copalyl diphosphate and contacting the CPP with a sclareol synthase enzyme to form (+)-manool and derivatives thereof. Also described herein are nucleic acids encoding CPP synthases and sclareol synthases for use in the methods. Further described herein are expression vectors and non-human host organisms and cells including nucleic acids encoding a CPP synthase and a sclareol synthase as described herein.

Abstract: Described herein is a method of producing a drimane sesquiterpene such as albicanol, drimenol and/or derivatives thereof by contacting at least one polypeptide with farnesyl diphosphate (FPP) with a polypeptide comprising a Haloacid dehalogenase (HAD)-like hydrolase domain and having bifunctional terpene synthase activity. The method may be performed in vitro or in vivo. Also described herein are amino acid sequences of polypeptides useful in the methods and nucleic acids encoding the polypeptides described. The described method further provides host cells or organisms genetically modified to express the polypeptides and useful to produce a drimane sesquiterpene such as albicanol, drimenol and/or derivatives thereof.

Abstract: Described herein are methods of producing (+)-manool, the methods including: contacting geranylgeranyl diphosphate with a copalyl diphosphate (CPP) synthase to form a (9S, 10S)-copalyl diphosphate and contacting the CPP with a sclareol synthase enzyme to form (+)-manool and derivatives thereof. Also described herein are nucleic acids encoding CPP synthases and sclareol synthases for use in the methods. Further described herein are expression vectors and non-human host organisms and cells including nucleic acids encoding a CPP synthase and a sclareol synthase as described herein.