This document describes biochemical pathways for producing 7-aminoheptanoic acid using a β-ketoacyl synthase or a β-ketothiolase to form either a 5-amino-3-oxopentanoyl-[ACP] or 5-amino-3-oxopentanoyl-CoA intermediate. 7-aminoheptanoic acid can be enzymatically converted to pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine or 1,7-heptanediol or the corresponding salts thereof. This document also describes recombinant microorganisms producing 7-aminoheptanoic acid as well as pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine and 1,7-heptanediol or the corresponding salts thereof.

An engineered microorganism(s) with novel pathways for the conversion of short-chain hydrocarbons to fuels and chemicals (e.g. carboxylic acids, alcohols, hydrocarbons, and their alpha-, beta-, and omega-functionalized derivatives) is described. Key to this approach is the use of hydrocarbon activation enzymes able to overcome the high stability and low reactivity of hydrocarbon compounds through the cleavage of an inert CH bond. Oxygen-dependent or oxygen-independent activation enzymes can be exploited for this purpose, which when combined with appropriate pathways for the conversion of activated hydrocarbons to key metabolic intermediates, enables the generation of product precursors that can subsequently be converted to desired compounds through established pathways. These novel engineered microorganism(s) provide a route for the production of fuels and chemicals from short chain hydrocarbons such as methane, ethane, propane, butane, and pentane.

Provided herein are methods, compositions, and non-naturally occurring microbial organism for preparing compounds such as 1-butanol, butyric acid, succinic acid, 1,4-butanediol, 1-pentanol, pentanoic acid, glutaric acid, 1,5-pentanediol, 1-hexanol, hexanoic acid, adipic acid, 1,6-hexanediol, 6-hydroxy hexanoic acid, -Caprolactone, 6-amino-hexanoic acid, -Caprolactam, hexamethylenediamine, linear fatty acids and linear fatty alcohols that are between 7-25 carbons long, linear alkanes and linear -alkenes that are between 6-24 carbons long, sebacic acid and dodecanedioic acid comprising: a) converting a C.sub.N aldehyde and pyruvate to a C.sub.N+3 -hydroxyketone intermediate through an aldol addition; and b) converting the C.sub.N+3 -hydroxyketone intermediate to the compounds through enzymatic steps, or a combination of enzymatic and chemical steps.

This document describes biochemical pathways for producing 7-aminoheptanoic acid using a -ketoacyl synthase or a -ketothiolase to form either a 5-amino-3-oxopentanoyl-[ACP] or 5-amino-3-oxopentanoyl-CoA intermediate. 7-aminoheptanoic acid can be enzymatically converted to pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine or 1,7-heptanediol or the corresponding salts thereof. This document also describes recombinant microorganisms producing 7-aminoheptanoic acid as well as pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine and 1,7-heptanediol or the corresponding salts thereof.

An engineered microorganism(s) with novel pathways for the conversion of short-chain hydrocarbons to fuels and chemicals (e.g. carboxylic acids, alcohols, hydrocarbons, and their alpha-, beta-, and omega-functionalized derivatives) is described. Key to this approach is the use of hydrocarbon activation enzymes able to overcome the high stability and low reactivity of hydrocarbon compounds through the cleavage of an inert CH bond. Oxygen-dependent or oxygen-independent activation enzymes can be exploited for this purpose, which when combined with appropriate pathways for the conversion of activated hydrocarbons to key metabolic intermediates, enables the generation of product precursors that can subsequently be converted to desired compounds through established pathways. These novel engineered microorganism(s) provide a route for the production of fuels and chemicals from short chain hydrocarbons such as methane, ethane, propane, butane, and pentane.

This document describes biochemical pathways for producing 1,3-butanediol using a polypetide having -ketothiolase activity to form a 3-oxo-5-hydroxypentanoyl-CoA intermediate that can be enzymatically converted to 1,3-butanediol, as well as recombinant hosts producing 1,3-butanediol.

The invention relates to a method to increase production of itaconic acid in a micro-organism by inhibiting the expression or functioning of the enzyme itaconyl-CoA transferase, itaconyl-CoA hydratase (citramalyl-CoA hydrolyase; EC 4.2.1.56) and/or citramalyl-CoA lyase. Also embodied are micro-organisms, preferably Aspergillus s terreus or Aspergillus niger, in which said enzyme is inhibited.

Described is a method for the production of isobutene from 3-methylcrotonyl-CoA comprising the steps of: (a) enzymatically converting 3-methylcrotonyl-CoA into 3-methylbutyric acid; and (b) further enzymatically converting the thus produced 3-methylbutyric acid into isobutene.

The conversion of 3-methylcrotonyl-CoA into 3-methylbutyric acid can be achieved by first enzymatically converting 3-methylcrotonyl-CoA into 3-methyl butyryl-CoA and further enzymatically converting the thus produced 3-methylbutyryl-CoA into 3-methylbutyric acid. Alternatively, the conversion of 3-methylcrotonyl-CoA into 3-methylbutyric acid can be achieved by first enzymatically converting 3-methylcrotonyl-CoA into 3-methylcrotonic acid and then further enzymatically converting the thus produced 3-methylcrotonic acid into 3-methylbutyric acid.

Described is a recombinant expression vector that enables a cell transformed to contain and express the vector to use levulinic acid as a carbon source, thereby converting levulnic acid into 2-butanne. Also described are genetically modified cells transformed to contain and express the vector and methods of using the cells to produce 2-butanone from a medium containing levulinic acid.

This document describes biochemical pathways for producing 1,3-butanediol using a polypetide having -ketothiolase activity to form a 3-oxo-5-hydroxypentanoyl-CoA intermediate that can be enzymatically converted to 1,3-butanediol, as well as recombinant hosts producing 1,3-butanediol.