# US 9,040,282 B2 · Producing dicarboxylic acids using polyketide synthases

> Agents: this data is available as JSON from the patentgrep API and MCP server — see https://patentgrep.com/llms.txt

- Number: US 9,040,282 B2
- Document ID: US9040282B2
- Status: Granted
- Kind: B2
- Application number: 14/038,488
- Filed: 2013-09-26
- Published: 2014-01-30
- Granted: 2015-05-26
- Earliest claimed: 2008-03-28
- Assignees: The Regents of the University of California
- Applicants: The Regents of the University of California
- Inventors: Leonard Katz; Jeffrey L Fortman; Jay D Keasling
- Web page: https://patentgrep.com/patent/US9040282B2

## CPC

- C12N 9/1029: {transferring groups other than amino-acyl groups (2.3.1)}
- C12N 9/10: Transferases (2.) (ribonucleases C12N9/22)
- C12N: MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA (microbiological testing media C12Q1/00)

## Abstract

The present invention provides for a polyketide synthase (PKS) capable of synthesizing a dicarboxylic acid (diacid). Such diacids include diketide-diacids and triketide-diacids. The invention includes recombinant nucleic acid encoding the PKS, and host cells comprising the PKS. The invention also includes methods for producing the diacids.

## Claims

### Claim 1

A recombinant polyketide synthase (PKS) capable of synthesizing a dicarboxylic acid (diacid), said PKS comprising a loading module containing a beta-keto acyl carrier protein synthase Q domain (KSQ) lacking decarboxylase activity, one or more extender modules and a thioesterase (TE) domain.

### Claim 2 (depends on 1)

The PKS of claim 1, wherein said diacid is pentane-1,5-dioic acid, and said PKS has a loading module that utilizes malonate and a single extender module that has a malonate-specific acyltransferase (AT) domain and a full set of reduction domains.

### Claim 3 (depends on 2)

The PKS of claim 2, wherein the loading module is from spiromycin, the single extender module is module 5 or module 6 from nystatin PKS or module 3 from the oligomycin PKS, and the TE domain is from erythromycin PKS.

### Claim 4 (depends on 1)

The PKS of claim 1, wherein said diacid is heptane-1,7-dioic acid; and said PKS has a loading module that utilizes malonate; a first and a second extender module, each of which has a malonate-specific acyltransferase (AT) domain; and a full set of reduction domains.

### Claim 5 (depends on 4)

The PKS of claim 4, wherein the loading module is from spiromycin, the first extender module is module 5 or module 6 from nystatin PKS or module 3 from the oligomycin PKS, the second extender module is module 5 from the epothilone PKS, and the TE domain is from erythromycin PKS.

### Claim 6 (depends on 1)

The PKS of claim 1, wherein said PKS comprises the loading module and module 1 of the spiramycin, oligomycin, or primaricin PKS; and the TE domain from erythromycin PKS or the TE domain encoded by the monCII gene; wherein the KSQ domain of the loading module is deleted or modified to inactivate the decarboxylase activity.

### Claim 7 (depends on 1)

The PKS of claim 1, wherein the diacid comprises from 1 to 10 ketide units.

### Claim 8 (depends on 7)

The PKS of claim 7, wherein the diacid comprises from 1 to 6 ketide units.

### Claim 9 (depends on 8)

The PKS of claim 8, wherein the diacid comprises from 1 to 3 ketide units.

### Claim 10 (depends on 9)

The PKS of claim 9, wherein the diacid is one described in Tables 2A-F and Tables 3A-KK.

### Claim 11 (depends on 1)

A host cell comprising the PKS of claim 1.

### Claim 12 (depends on 11)

The host cell of claim 11, wherein the host cell is a prokaryotic host cell.

### Claim 13 (depends on 12)

The host cell of claim 12, wherein the prokaryotic host cell is an E. coli or a Streptomyces sp. cell.

### Claim 14 (depends on 11)

The host cell of claim 11, wherein the host cell is a yeast host cell.