Genetically modified isopropylmalate isomerase enzyme complexes (e.g., LeuCD enzyme complexes), microbial organisms including genetically modified isopropylmalate isomerase enzyme complexes (e.g., LeuCD), and processes for preparing C7-C11 2-ketoacids with genetically modified isopropylmalate isomerase enzyme complexes (e.g., LeuCD). The genetically modified isopropylmalate isomerase enzyme complexes (e.g., LeuCD enzyme complexes), microbial organisms, and processes for preparing C7-C11 2-ketoacids can be used to produce C6-C10 aldehydes, alkanes, alcohols, and carboxylic acids, both in vivo and in vitro.

Genetically modified LeuCD enzyme complexes, processes for preparing a C.sub.7-C.sub.11 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 C.sub.7-C.sub.11 2-ketoacid, and microbial organisms including modified LeuCD enzyme complexes can be particularly useful for producing C.sub.6-C.sub.10 aldehydes, alkanes, alcohols, and carboxylic acids, both in vivo and in vitro.

Genetically modified isopropylmalate synthases, processes for preparing a C.sub.7-C.sub.11 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 C.sub.7-C.sub.11 2-ketoacids, and microbial organisms including genetically modified isopropylmalate synthases can be particularly useful for producing corresponding C.sub.n.sub._.sub.1 aldehydes, alcohols, carboxylic acids, and C.sub.n.sub._.sub.2 alkanes both in vivo and in vitro.

The present application relates to a microorganism of the genus Corynebacterium having L-isoleucine producing ability which comprises a protein having an activity of citramalate synthase, and a method for producing L-isoleucine using the same.

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. This genetic engineering offers the opportunity for commercial scale of in vivo biosynthetic processes that may be more cost-efficient than non-biobased approaches to produce the same products.

This document describes biochemical pathways for producing pimelic acid, 7-aminoheptanoic acid, 7-hydroxyheptanoic acid, heptamethylenediamine or 1,7-heptanediol by forming one or two terminal functional groups, each comprised of carboxyl, amine or hydroxyl group, in a C7 aliphatic backbone substrate. These pathways, metabolic engineering and cultivation strategies described herein rely on the C1 elongation enzymes or homolog associated with coenzyme B biosynthesis.

This document describes biochemical pathways for producing pimelic acid, 7-aminoheptanoic acid, 7-hydroxyheptanoic acid, heptamethylenediamine or 1,7-heptanediol by forming one or two terminal functional groups, each comprised of carboxyl, amine or hydroxyl group, in a C7 aliphatic backbone substrate. These pathways, metabolic engineering and cultivation strategies described herein rely on the C1 elongation enzymes or homolog associated with coenzyme B biosynthesis.

The present invention provides a method for producing 2-methyl-butyric acid by fermentation using a bacterium belonging to the order Enterobacterales which has been modified to attenuate expression of a tyrB gene encoding a protein having tyrosine aminotransferase activity. The method also allows for production of a byproduct substance of 2-methyl-butyric acid during fermentation of the Enterobacterales bacterium having 2-methyl-butyric acid-producing ability.

The present invention relates to preparation of key drug intermediate, L-2-amino butyric acid (L-2-ABA) by a method of cell free system and biotransformation using genetically engineered strains from easily available economic substrates like citramalate or citraconate and enzymes like LeuCD, LeuB and ValDH or IlvE.