Invista North America S.a.r.l.

Inv Nylon Chemicals Americas, LLC

Nadia Fatma Kadi

Adriana Leonora Botes

Alex Van Eck Conradie

Alexandre Zanghellini

Eric Anthony Althoff

Daniela Grabs-Röthlisberger

Mihai Luchian Azoitei

Yih-En Andrew Ban

Alexander Pisarchik

Alexander Brett Foster

Adriana Leonara Botes

Mariusz Kamionka

Jonathan Kennedy

This document describes biochemical pathways for producing 7-aminoheptanoic acid using a &#x3b2;-ketoacyl synthase or a &#x3b2;-ketothiolase to form an N-acetyl-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 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 corresponding salts thereof.

Methods and materials for producing 7-carbon monomers

This document describes biochemical pathways for producing 7-aminoheptanoic acid using a &#x3b2;-ketoacyl synthase or a &#x3b2;-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.

This document describes polypeptides with dual CoA transferase and &#x3b2;-ketothiolase activities and variants thereof, use of such polypeptides in biosynthetic methods, and non-naturally occurring hosts comprising such polypeptides.

Polypeptides for carbon-carbon bond formation and uses thereof

The present disclosure provides novel polypeptides with 3-buten-2-ol dehydratase activity, polypeptides with catalytic activity in the conversion of 3-methyl-3-buten-2-ol to isoprene, and crystal structure data for one of such polypeptides. Methods of making and using the polypeptides and their related crystal structure data are also provided.

Mutant polypeptides and uses thereof

This document describes materials and methods for, for example, producing 6-hydroxyhexanoic acid using a &#x3b2;-ketothiolase or synthase and an alcohol O-acetyltransferase to form a 6-acetyloxy-3-oxohexanoyl-CoA intermediate. This document describes biochemical pathways for producing 6-hydroxyhexanoic acid using a &#x3b2;-ketothiolase or synthase and an alcohol O-acetyltransferase to form a 6-acetyloxy-3-oxohexanoyl-CoA intermediate. 6-hydroxyhexanoic acid can be enzymatically converted to adipic acid, caprolactam, 6-aminohexanoic acid, hexamethylenediamine or 1,6-hexanediol. This document also describes recombinant hosts producing 6-hydroxyhexanoic acid as well as adipic acid, caprolactam, 6-aminohexanoic acid, hexamethylenediamine and 1,6-hexanediol.

Materials and methods for producing 6-carbon monomers

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.

Methods, reagents and cells for biosynthesizing glutarate methyl ester

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].

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Middlesbrough, United Kingdom

Nadia Fatma Kadi