The invention provides a genetically modified bacterial cell capable of improved iron-sulfur cluster delivery, characterized by a modified gene encoding a mutant Iron Sulfur Cluster Regulator (IscR) as well as one or more transgenes encoding polypeptides that enhance the biosynthesis of either biotin, lipoic acid or thiamine. The invention provides a method for producing either biotin, lipoic acid or thiamine using the genetically modified bacterium of the invention; as well as for the use of the genetically modified bacterial cell for either biotin, lipoic acid or thiamine production.

A bacterium of the species Corynebacterium glutamicum has the ability to excrete L-lysine, and contains in its chromosome a polynucleotide encoding a mutated polypeptide having the assumed function of an acyltransferase, hydrolase, alpha/beta hydrolase or of a pimeloyl-ACP methyl ester esterase. Also, a method is used for producing L-lysine using such bacterium.

The invention provides a process for reacting a carboxylic acid ester of the formula (I)
R.sup.1-A-COOR.sup.2(I), wherein R.sup.1 is hydrogen, CH.sub.2OH, CHO, COOR.sup.3, CH.sub.2SH, CH.sub.2OR.sup.3 or CH.sub.2NH.sub.2, R.sup.2 is an alkyl group, R.sup.3 is hydrogen or an alkyl group, and A is a substituted, unsubstituted, linear, branched and/or cyclic alkylene, alkenylene, arylene or aralkylene radical having at least 4 carbons, in the presence of a cell. The process comprises a) contacting the cell with said carboxylic acid ester in an aqueous solution, wherein the cell is a recombinant cell which has reduced activity of a polypeptide comprising SEQ ID NO: 2 or a variant thereof over the wild-type cell.

A bacterium of the species Corynebacterium glutamicum has the ability to excrete L-lysine, and contains in its chromosome a polynucleotide encoding a mutated polypeptide having the assumed function of an acyltransferase, hydrolase, alpha/beta hydrolase or of a pimeloyl-ACP methyl ester esterase. Also, a method is used for producing L-lysine using such bacterium.

This document describes biochemical pathways for producing 2,4-pentadienoyl-CoA by forming one or two terminal functional groups, comprised of carboxyl or hydroxyl group, in a C5 backbone substrate such as glutaryl-CoA, glutaryl-[acp] or glutarate methyl ester. 2,4-pentadienoyl-CoA can be enzymatically converted to 1,3-butadiene.

This document describes biochemical pathways for producing 2,3-dehydroadipyl-CoA methyl ester from precursors such as 2-oxoglutarate using one or more of a fatty acid O-methyltransferase, a thioesterase, a CoA-transferase and a CoA ligase, as well as recombinant hosts expressing one or more of such enzymes. 2,3-dehydroadipyl-CoA methyl ester can be enzymatically converted to adipyl-CoA using a trans-2-enoyl-CoA reductase, and a methylesterase, which in turn can be enzymatically converted to adipic acid, 6-aminohexanoate, 6-hydroxyhexanoate, caprolactam, hexamethylenediamine, or 1,6-hexanediol.

This document describes biochemical pathways for producing 2,4-pentadienoyl-CoA by forming one or two terminal functional groups, comprised of carboxyl or hydroxyl group, in a C5 backbone substrate such as glutaryl-CoA, glutaryl-[acp] or glutarate methyl ester. 2,4-pentadienoyl-CoA can be enzymatically converted to 1,3-butadiene.

This document describes biochemical pathways for producing glutaric acid, 5-aminopentanoic acid, 5-hydroxypentanoic acid, cadaverine or 1,5-pentanediol by forming one or two terminal functional groups, comprised of carboxyl, amine or hydroxyl group, in a C5 backbone substrate such as malonyl-CoA or malonyl-[acp].

This document describes biochemical pathways for producing 2(E)-heptenedioyl-CoA methyl ester from precursors such as 2-oxo-glutarate, acetyl-CoA, or succinyl-CoA using one or more of a fatty acid O-methyltransferase, a thioesterase, a CoA-transferase, a CoA ligase, as well as recombinant hosts expressing one or more of such enzymes. 2(E)-heptenedioyl-CoA methyl ester can be enzymatically converted to pimeloyl-CoA using a trans-2-enoyl-CoA reductase, and a methylesterase. Pimeloyl-CoA can be enzymatically converted to pimelic acid, 7-aminoheptanoate, 7-hydroxyheptanoate, heptamethylenediamine, or 1,7-heptanediol.

This document describes biochemical pathways for producing 2,4-pentadienoyl-CoA by forming one or two terminal functional groups, comprised of carboxyl or hydroxyl group, in a C5 backbone substrate such as glutaryl-CoA, glutaryl-[acp] or glutarate methyl ester. 2,4-pentadienoyl-CoA can be enzymatically converted to 1,3-butadiene.