IP Library › Granted Patent US 12,545,937
Granted Patent B2
US 12,545,937 · App. 18/274,912 · Granted Feb 10, 2026

Isopropylmalate synthase variant and a method of producing L-leucine using the same

Inventors: Hayun Lee (Seoul, KR); Ju Eun Kim (Seoul, KR); Ji Hye Lee (Seoul, KR)
Assignee: CJ CHEILJEDANG CORPORATION
C12P13/06C12N9/1025C12N15/77C12R2001/15C12Y203/03013
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 12,545,937
App. No.
18/274,912
Granted
Feb 10, 2026
Kind
B2
Abstract

The present disclosure relates to an isopropylmalate synthase variant and a method of producing L-leucine using the same.

Claims (16)

1 . A polypeptide variant having an isopropylmalate synthase activity, comprising one or more substitutions selected from the group consisting of i) a substitution of an amino acid residue corresponding to position 138 with another amino acid residue, ii) a substitution of an amino acid residue corresponding to position 162 with another amino acid residue, iii) a substitution of an amino acid residue corresponding to position 211 with another amino acid residue, iv) a substitution of an amino acid residue corresponding to position 245 with another amino acid residue, and v) a substitution of an amino acid residue corresponding to position 588 with another amino acid residue, in the amino acid sequence of SEQ ID NO: 1.

2 . The polypeptide variant of claim 1 , wherein i) leucine, which is the amino acid residue corresponding to position 138, is substituted with glycine.

3 . The polypeptide variant of claim 1 , wherein ii) histidine, which is the amino acid residue corresponding to position 162, is substituted with glutamate.

4 . The polypeptide variant of claim 1 , wherein iii) serine, which is the amino acid residue corresponding to position 211, is substituted with leucine.

5 . The polypeptide variant of claim 1 , wherein iv) asparagine, which is the amino acid residue corresponding to position 245, is substituted with serine.

6 . The polypeptide variant of claim 1 , wherein v) isoleucine, which is the amino acid residue corresponding to position 588, is substituted with proline.

7 . The polypeptide variant of claim 1 , comprising any one or more amino acid sequences selected from the group consisting of SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 10, SEQ ID NO: 12, and SEQ ID NO: 14.

8 . A polynucleotide encoding the polypeptide variant of claim 1 .

9 . A vector comprising the polynucleotide of claim 8 .

10 . A microorganism of the genus Corynebacterium producing L-leucine, the microorganism comprising the polypeptide variant of claim 1 ; a polynucleotide encoding the same;

or a vector including the same.

11 . The microorganism of the genus Corynebacterium of claim 10 , wherein the microorganism of the genus Corynebacterium is Corynebacterium glutamicum.

12 . A method of producing L-leucine, the method comprising a step of culturing, in a medium, a microorganism of the genus Corynebacterium producing L-leucine, the microorganism comprising the polypeptide variant of claim 1 ; a polynucleotide encoding the same; or a vector including the same.

13 . The method of claim 12 , further comprising a step of recovering L-leucine from the medium or from the microorganism after the step of culturing.

14 . A composition for producing L-leucine, the composition comprising a microorganism of genus Corynebacterium producing L-leucine, the microorganism comprising the polypeptide variant of claim 1 , a polynucleotide encoding the same, or a vector including the same; or a medium in which the microorganism is cultured.

15 . The polypeptide variant according to claim 1 , comprising at least 80% sequence identity to SEQ ID NO: 1.

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Feb 14, 2024
From: LEE, HAYUN; KIM, JU EUN; LEE, JI HYE
To: CJ CHEILJEDANG CORPORATION
Reel/Frame 066459/0657 →
Priority Claims (1)
KR 10-2021-0029469 · Mar 5, 2021 · national
Continuity (1)
Related Publication 20240093252A1 · Mar 21, 2024
References Cited (24)
US 6403342B1 · Gusyatiner et al. · 2002 [cited by applicant]
US 7662943B2 · Park et al. · 2010 [cited by applicant]
US 10273491B2 · Lee et al. · 2019 [cited by applicant]
US 10584338B2 · Lee et al. · 2020 [cited by applicant]
US 20150079641A1 · Gerstmeir et al. · 2015 [cited by applicant]
US 20210189354A1 · Zhang et al. · 2021 [cited by applicant]
US 20210254111A1 · Lee et al. · 2021 [cited by applicant]
EP 1067191A2 · 2001 [cited by applicant]
EP 1568776A2 · 2005 [cited by applicant]
EP 2841568A1 · 2015 [cited by applicant]
EP 3564366A2 · 2019 [cited by applicant]
EP 4155395A1 · 2023 [cited by applicant]
JP 2015514431A · 2015 [cited by applicant]
JP 2020503045A · 2020 [cited by applicant]
KR 100220018B1 · 1999 [cited by applicant]
KR 100438146B1 · 2004 [cited by applicant]
KR 1020140067082A · 2014 [cited by applicant]
KR 1020180077008A · 2018 [cited by applicant]
Office Action issued in corresponding Japanese Patent Application No. 2023-540849, dated Jul. 30, 2024. [cited by applicant]
Extended European Search Report in corresponding European Patent Application No. 22763472.2, dated May 24, 2024. [cited by applicant]
Vogt et al., “Pushing product formation to its limit: Metabolie engineering of Corynebacterium glutamicum for l-leucine overproduction”, Metabolic Engineering, vol. 22, No. 1, Mar. 2014, pp. 40-52, XP055111480. [cited by applicant]
Kohlhaw, “Leucine Biosynthesis in Fungi: Entering Metabolism through the Back Door,” Microbiology and Molecular Biology Reviews, 67(1): 1-15 (2003). [cited by applicant]
International Search Report issued in corresponding International Patent Application No. PCT/KR2022/001560 dated May 16, 2022. [cited by applicant]
Office Action issued in corresponding Brazilian Patent Application No. BR112023015182-1, dated Oct. 1, 2024. [cited by applicant]