Abstract: Genetically modified LeuCD? enzyme complexes, processes for preparing a C7-C11 2-ketoacid utilizing genetically modified LeuCD? enzyme complexes, and microbial organisms including modified LeuCD enzyme complexes are described. The instantly-disclosed genetically modified LeuCD? enzyme complexes, processes for preparing a C7-C11 2-ketoacid, and microbial organisms including modified LeuCD? enzyme complexes can be particularly useful for producing C6-C10 aldehydes, alkanes, alcohols, and carboxylic acids, both in vivo and in vitro.

Abstract: Genetically modified isopropylmalate synthases, processes for preparing a C7-C11 2-ketoacids utilizing genetically modified isopropylmalate synthases, and microbial organisms including genetically modified isopropylmalate synthases are described. The genetically modified isopropylmalate synthases, processes for preparing a C7-C11 2-ketoacids, and microbial organisms including genetically modified isopropylmalate synthases can be particularly useful for producing corresponding Cn_1 aldehydes, alcohols, carboxylic acids, and Cn_2 alkanes both in vivo and in vitro.

Abstract: Genetically modified LeuCD? enzyme complexes, processes for preparing a C7-C11 2-ketoacid utilizing genetically modified LeuCD? enzyme complexes, and microbial organisms including modified LeuCD enzyme complexes are described. The instantly-disclosed genetically modified LeuCD? enzyme complexes, processes for preparing a C7-C11 2-ketoacid, and microbial organisms including modified LeuCD? enzyme complexes can be particularly useful for producing C6-C10 aldehydes, alkanes, alcohols, and carboxylic acids, both in vivo and in vitro.

Abstract: Genetically modified isopropylmalate synthases, processes for preparing a C7-C11 2-ketoacids utilizing genetically modified isopropylmalate synthases, and microbial organisms including genetically modified isopropylmalate synthases are described. The genetically modified isopropylmalate synthases, processes for preparing a C7-C11 2-ketoacids, and microbial organisms including genetically modified isopropylmalate synthases can be particularly useful for producing corresponding Cn_1 aldehydes, alcohols, carboxylic acids, and Cn_2 alkanes both in vivo and in vitro.

Abstract: Modification of the amino acid sequence of a phenylpyruvate decarboxylase from Azospirillum brasilense produces a novel group of phenylpyruvate decarboxylases with improved specificity to certain substrates, including in particular C7-C11 2-ketoacids such as, for example, 2-ketononanoate and 2-keto-octanoate. This specificity enables effective use of the phenylpyruvate decarboxylase in, for example, an in vivo process wherein 2-ketobutyrate or 2-ketoisovalerate are converted to C7-C11 2-ketoacids, and the novel phenylpyruvate decarboxylase converts the C7-C11 2-ketoacid to a C6-C10 aldehyde having one less carbon than the 2-ketoacid. Ultimately, through contact with additional enzymes, such C6-C10 aldehydes may be converted to, for example, C6-C10 alcohols, C6-C10 carboxylic acids, C6-C10 alkanes, and other derivatives. Use of the novel genetically modified phenylpyruvate decarboxylases may represent a lower cost alternative to non-biobased approaches.

Abstract: Modification of metabolic pathways includes genetically engineering at least one enzyme involved in elongating 2-ketoacids during leucine biosynthesis, and preferably at least isopropylmalate dehydrogenase or synthase (LeuB or LeuA in E. coli), to include at least such non-native enzyme, enzyme complex, or combination thereof to convert 2-ketobutyrate or 2-ketoisovalerate to a C7-C11 2-ketoacid, wherein the production of such is at a higher efficiency than if a purely native pathway is followed. The C7-C11 2-ketoacid may then be converted, via a native or genetically engineered thiamin dependent decarboxylase, to form a C6-C10 aldehyde having one less carbon than the C7-C11 2-ketoacid being converted. In some embodiments the C6-C10 aldehyde may then be converted via additional native or genetically engineered enzymes to form other C6-C10 products, including alcohols, carboxylic acids, and alkanes.

Abstract: Modification of the amino acid sequence of a phenylpyruvate decarboxylase from Azospirillum brasilense produces a novel group of phenylpyruvate decarboxylases with improved specificity to certain substrates, including in particular C7-C11 2-ketoacids such as, for example, 2-ketononanoate and 2-keto-octanoate. This specificity enables effective use of the phenylpyruvate decarboxylase in, for example, an in vivo process wherein 2-ketobutyrate or 2-ketoisovalerate are converted to C7-C11 2-ketoacids, and the novel phenylpyruvate decarboxylase converts the C7-C11 2-ketoacid to a C6-C10 aldehyde having one less carbon than the 2-ketoacid. Ultimately, through contact with additional enzymes, such C6-C10 aldehydes may be converted to, for example, C6-C10 alcohols, C6-C10 carboxylic acids, C6-C10 alkanes, and other derivatives. Use of the novel genetically modified phenylpyruvate de carboxylases may represent a lower cost alternative to non-biobased approaches.

Abstract: Modification of metabolic pathways includes genetically engineering at least one enzyme involved in elongating 2-ketoacids during leucine biosynthesis, and preferably at least isopropylmalate dehydrogenase or synthase (LeuB or LeuA in E. coli), to include at least such non-native enzyme, enzyme complex, or combination thereof to convert 2-ketobutyrate or 2-ketoisovalerate to a C7-C11 2-ketoacid, wherein the production of such is at a higher efficiency than if a purely native pathway is followed. The C7-C11 2-ketoacid may then be converted, via a native or genetically engineered thiamin dependent decarboxylase, to form a C6-C10 aldehyde having one less carbon than the C7-C11 2-ketoacid being converted. In some embodiments the C6-C10 aldehyde may then be converted via additional native or genetically engineered enzymes to form other C6-C10 products, including alcohols, carboxylic acids, and alkanes.