IP Library Granted Patent US 12,649,909
Granted Patent B2
US 12,649,909 · App. 18/279,519 · Granted Jun 9, 2026

Citrate synthase variant and method for producing O-acetyl-L-homoserine or L-methionine using same

Inventors: Jin Sook Chang (Seoul, KR); Seung Hyun Cho (Seoul, KR); Seo-Yun Kim (Seoul, KR); Jaemin Lee (Seoul, KR); Min Ji Baek (Seoul, KR); Imsang Lee (Seoul, KR)
Assignee: CJ CHEILJEDANG CORPORATION
C12N9/1025C12N15/77C12P13/06C12P13/12C12R2001/15C12Y203/03001
View Patent ↗
Loading inventors, assignments & file history…
Monitor This Case
Get email alerts when status or documents change.
Order Certified Copies
Most orders are placed with the USPTO same day — all within 24 business hours.
Order via The Patent Place →
Pre-filled with this patent's details
Quick Facts
Patent No.
US 12,649,909
App. No.
18/279,519
Granted
Jun 9, 2026
Kind
B2
Abstract

The present disclosure relates to a citrate synthase variant, a microorganism comprising the variant, and a method for producing O-acetyl-L-homoserine and L-methionine using the microorganism.

Claims (28)

1 . A citrate synthase variant having citrate synthase activity,

wherein the amino acid at position corresponding to position 415 of the polypeptide of SEQ ID NO: 1 is histidine,

the amino acid at the position corresponding to position 241 of the polypeptide of SEQ ID NO: 1 is threonine, and

the variant has an amino acid sequence at least 95% identical to SEQ ID NO: 1.

2 . The variant of claim 1 , wherein the variant comprises the amino acid sequence of SEQ ID NO: 6.

3 . The variant of claim 1 , wherein the variant comprises the amino acid sequence of SEQ ID NO: 33, in which the amino acid at position 1 of SEQ ID NO: 33 is asparagine or a serine, the amino acid at position 9 of SEQ ID NO: 33 is alanine or glutamic acid, and the amino acid at position 73 of SEQ ID NO: 33 is tyrosine or cysteine.

4 . The variant of claim 1 , wherein the variant comprises an amino acid sequence at least 95% identical to SEQ ID NO: 6.

5 . A polynucleotide encoding a citrate synthase variant having citrate synthase activity,

wherein the amino acid at position corresponding to position 415 of the polypeptide of SEQ ID NO: 1 is histidine,

the amino acid at the position corresponding to position 241 of the polypeptide of SEQ ID NO: 1 is threonine, and

the variant has an amino acid sequence at least 95% identical to SEQ ID NO: 1.

6 . A microorganism of the genus Corynebacterium , comprising

(a) a citrate synthase variant having citrate synthase activity, wherein the amino acid at the position corresponding to position 415 of the polypeptide of SEQ ID NO: 1 is histidine, the amino acid at the position corresponding to position 241 of the polypeptide of SEQ ID NO: 1 is threonine, and the variant has an amino acid sequence at least 95% identical to SEQ ID NO: 1; or

(b) a polynucleotide encoding the citrate synthase variant of (a).

7 . The microorganism of claim 6 , wherein the microorganism has an O-acetyl-L-homoserine-producing ability.

8 . The microorganism of claim 6 , wherein the microorganism is Corynebacterium glutamicum.

9 . A method for producing O-acetyl-L-homoserine or L-methionine, comprising culturing the microorganism of claim 6 in a medium.

10 . The method of claim 9 , wherein the method further comprises recovering O-acetyl-L-homoserine or L-methionine from the cultured medium or microorganism.

11 . The method of claim 9 , wherein the method for producing L-methionine further comprises converting the O-acetyl-L-homoserine into L-methionine.

12 . A composition for producing O-acetyl-L-homoserine or L-methionine, that comprises the microorganism of claim 6 and a growth medium.

13 . The variant of claim 1 , wherein the variant comprises an amino acid sequence at least 98% identical to SEQ ID NO: 1.

14 . The variant of claim 1 , wherein the variant comprises an amino acid sequence at least 99% identical to SEQ ID NO: 1.

15 . A microorganism comprising the variant of claim 1 .

16 . A microorganism comprising the variant of claim 5 .

17 . A method for producing O-acetyl-L-homoserine or L-methionine, comprising culturing the microorganism of claim 16 in a medium.

18 . The method of claim 17 , wherein the method further comprises recovering O-acetyl-L-homoserine or L-methionine from the cultured medium or microorganism.

19 . A method for producing O-acetyl-L-homoserine or L-methionine, comprising culturing the microorganism of claim 15 in a medium.

20 . The method of claim 19 , wherein the method further comprises recovering O-acetyl-L-homoserine or L-methionine from the cultured medium or microorganism.

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Sep 14, 2023
From: CHANG, JIN SOOK; CHO, SEUNG HYUN; KIM, SEO-YUN; LEE, JAEMIN; BAEK, MIN JI; LEE, IMSANG
To: CJ CHEILJEDANG CORPORATION
Reel/Frame 064905/0118 →
Priority Claims (1)
KR 10-2021-0031643 · Mar 10, 2021 · national
Continuity (1)
Related Publication 20240150730A1 · May 9, 2024
References Cited (26)
US 7662943B2 · Park et al. · 2010 [cited by applicant]
US 8283152B2 · Kim et al. · 2012 [cited by applicant]
US 8426171B2 · Kim et al. · 2013 [cited by applicant]
US 10273491B2 · Lee et al. · 2019 [cited by applicant]
US 10584338B2 · Lee et al. · 2020 [cited by applicant]
US 20080014618A1 · Bathe et al. · 2008 [cited by applicant]
JP 2016526927A · 2016 [cited by applicant]
JP 2018528771A · 2018 [cited by applicant]
KR 1019920007401B1 · 1992 [cited by applicant]
KR 101641770B1 · 2016 [cited by applicant]
KR 101915433B1 · 2018 [cited by applicant]
KR 1020200136813A · 2020 [cited by applicant]
WO 2006065095A1 · 2006 [cited by applicant]
WO 2016526927A · 2019 [cited by applicant]
Witkowski et al., Biochemistry 38:11643-11650, 1999. [cited by examiner]
Tang et al., Phil Trans R Soc B 368:20120318, 1-10, 2013. [cited by examiner]
Seffernick et al., J. Bacteriol. 183(8):2405-2410, 2001. [cited by examiner]
Singh et al., Current Protein and Peptide Science 19(1):5-15, 2018. [cited by examiner]
Sadowski et al., Current Opinion in Structural Biology 19:357-362, 2009. [cited by examiner]
NCBI, GenBank accession No. WP_011013914.1 citrate synthase [Corynebacterium glutamicum] (Nov. 28, 2019). [cited by applicant]
Van Ooyen et al., “Improved L-Lysine Production With Corynebacterium glutamicum and Systemic Insight Into Citrate Synthase Flux and Activity,” Biotechnology and Bioengineering, 109(8): 2070-2081 (2012). [cited by applicant]
Edelheit et al., “Simple and efficient site-directed mutagenesis using two single-primer reactions in parallel to generate mutants for protein structure-function studies,” BMC Biotechnology, 9(61): 1-8 (2009). [cited by applicant]
Needleman et al., “A General Method Applicable to the Search for Similarities in the Amino Acid Sequence of Two Proteins,” Journal of Molecular Biology, 48(3): 443-453 (1970). [cited by applicant]
Devereux et al., “A comprehensive set of sequence analysis programs for the VAX,” Nucleic Acids Research, 12(1): 387-395 (1984). [cited by applicant]
International Search Report issued in corresponding International Patent Application No. PCT/KR2022/003357 dated Jul. 6, 2022 . [cited by applicant]
Office Action issued in corresponding Japanese Patent Application No. 2023-548892 dated Aug. 6, 2024. [cited by applicant]