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.

A method of producing lipids, comprising the steps of: culturing a transformant in which the expression of a gene encoding at least any one of the following proteins (A) to (D) is enhanced in a cyanobacteria cell, and producing fatty acids or lipids containing these fatty acids as components. (A) a protein consisting of the amino acid sequence set forth in SEQ ID NO: 1; (B) a protein consisting of an amino acid sequence having 60% or more identity with the amino acid sequence of the protein (A), and having -ketoacyl-ACP synthase activity; (C) a protein consisting of the amino acid sequence set forth in SEQ ID NO: 44; and (D) a protein consisting of an amino acid sequence having 60% or more identity with the amino acid sequence of the protein (C), and having -ketoacyl-ACP synthase activity.

Disclosed herein are methods and compositions that enable the production of branched-chain polyhydroxyalkanoates, branched-chain 3-hydroxyacids (BCHA) (PHA monomers), and branched-chain fatty acids (BCFA) in Pseudomonas putida KT2440. The branched-chain molecules enabled by this platform enable novel chemistries that are not accessible via the existing paradigm which is limited to straight-chain molecules.

Further disclosed herein are methods and compositions for deciphering the mechanisms of bacterial fatty acid biosynthesis is crucial for both the engineering of bacterial hosts to produce fatty acid-derived molecules and the development of new antibiotics.

A method of producing a long-chain fatty alcohol, containing culturing a microorganism wherein expression of a gene encoding a 3-ketoacyl-ACP synthase and expression of a gene encoding a fatty acyl-CoA reductase are enhanced; a method of providing ability to produce a long-chain fatty alcohol for a microorganism wherein expression of a gene encoding a 3-ketoacyl-ACP synthase and expression of a gene encoding a fatty acyl-CoA reductase are enhanced in a microorganism cell; and a transformant of a microorganism in which expression of a gene encoding a -ketoacyl-ACP synthase and expression of a gene encoding a fatty acyl-CoA reductase are enhanced.

A recombinant cell for producing a fatty acid ester. The recombinant cell is genetically engineered to produce a reduction in free fatty acids compared to a cell that has not been similarly genetically engineered. Methods for producing fatty acid esters while decreasing free fatty acid production are also described.

Disclosed herein, in some embodiments, are vectors encoding biosynthetic enzymes from gut microbiome-derived bacterium (e.g., Clostridia enzymes), engineered cells comprising the vectors, and methods of using biosynthetic enzymes from gut microbiome-derived bacterium (e.g., Clostridia enzymes) to produce fatty acid amides.

A method of producing lipids, containing the steps of: culturing a transformant into which a gene encoding at least one protein selected from the group consisting of the following proteins (A) to (C) is introduced; and producing fatty acids or lipids containing the same as components: (A) a protein consisting of an amino acid sequence having at least one amino acid substitution selected from the group consisting of the following (A-1) to (A-11) in the amino acid sequence set forth in SEQ ID NO: 1, and having acyl-ACP thioesterase activity; (B) a protein consisting of an amino acid sequence having at least one amino acid substitution selected from the group consisting of the following (B-1) to (B-11) in an amino acid sequence having 85% or more identity with the amino acid sequence set forth in SEQ ID NO: 1, and having acyl-ACP thioesterase activity; and (C) a protein containing the amino acid sequence of the protein (A) or (B), and having acyl-ACP thioesterase activity: (A-1) substitution of isoleucine for leucine at position 257 of the amino acid sequence set forth in SEQ ID NO: 1; (A-2) substitution of arginine for threonine at position 251 of the amino acid sequence set forth in SEQ ID NO: 1; (A-3) substitution of lysine for threonine at position 251 of the amino acid sequence set forth in SEQ ID NO: 1; (A-4) substitution of histidine for threonine at position 251 of the amino acid sequence set forth in SEQ ID NO: 1; (A-5) substitution of isoleucine for tryptophan at position 254 of the amino acid sequence set forth in SEQ ID NO: 1; (A-6) substitution of tyrosine for tryptophan at position 254 of the amino acid sequence set forth in SEQ ID NO: 1; (A-7) substitution of methionine for leucine at position 257 of the amino acid sequence set forth in SEQ ID NO: 1; (A-8) substitution of valine for leucine at position 257 of the amino acid sequence set forth in SEQ ID NO: 1; (A-9) substitution of phenylalanine for leucine at position 257 of the amino acid sequence set forth in SEQ ID NO: 1; (A-10) substitution of cysteine for valine at position 266 of the amino acid sequence set forth in SEQ ID NO: 1; (A-11) substitution of tyrosine for tryptophan at position 271 of the amino acid sequence set forth in SEQ ID NO: 1; (B-1) substitution of isoleucine for an amino acid at a position corresponding to position 257 of the amino acid sequence set forth in SEQ ID NO: 1; (B-2) substitution of arginine for an amino acid at a position corresponding to position 251 of the amino acid sequence set forth in SEQ ID NO: 1; (B-3) substitution of lysine for an amino acid at a position corresponding to position 251 of the amino acid sequence set forth in SEQ ID NO: 1; (B-4) subst

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.

A method of improving lipid productivity, containing the steps of: enhancing the expression of a gene encoding the following protein (A) or (B), and improving the productivity of medium-chain fatty acids or lipids containing these fatty acids as components produced in a cell of a transformant, or the total amount of all fatty acids produced in a cell of a transformant:
(A) a protein consisting of the amino acid sequence set forth in SEQ ID NO: 1; and
(B) a protein consisting of an amino acid sequence having 64% or more identity with the amino acid sequence of the protein (A), and having glycerol-3-phosphate dehydrogenase activity.

The present invention is directed to isolated nucleic acid molecules and polypeptides of thraustochytrid polyunsaturated fatty acid (PUFA) synthases involved in the production of PUFAs, including PUFAs enriched in docosahexaenoic acid (DHA), eicosapentaenoic acid (EPA), or a combination thereof. The present invention is directed to vectors and host cells comprising the nucleic acid molecules, polypeptides encoded by the nucleic acid molecules, compositions comprising the nucleic acid molecules or polypeptides, and methods of making and uses thereof.