Aspartokinase variant and method for producing L-amino acid using the same
US-10662450-B2 · May 26, 2020 · US
Modified polypeptide with attenuated activity of citrate synthase and method for producing L-amino acid using the same
US12522808B2 · US · B2
| Field | Value |
|---|---|
| Publication number | US-12522808-B2 |
| Application number | US-202017779909-A |
| Country | US |
| Kind code | B2 |
| Filing date | Aug 4, 2020 |
| Priority date | Jan 30, 2020 |
| Publication date | Jan 13, 2026 |
| Grant date | Jan 13, 2026 |
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Abstract
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The present disclosure relates to a modified polypeptide with attenuated activity of citrate synthase, a microorganism producing leucine comprising the modified polypeptide, and a method for producing an L-amino acid using the microorganism.
First claim
Opening claim text (preview).
The invention claimed is: 1 . A modified polypeptide having citrate synthase activity, wherein the amino acid corresponding to the 312 th position from the N-terminus of the amino acid sequence of SEQ ID NO: 1 is substituted with alanine, arginine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, histidine, isoleucine, leucine, lysine, phenylalanine, proline, serine, threonine, tryptophan, tyrosine or valine, wherein the amino acid sequence of the modified polypeptide shares at least 80% but less than 100% sequence identity with the amino acid sequence of SEQ ID NO: 1. 2 . The modified polypeptide of claim 1 , wherein the modified polypeptide comprisesis the amino acid sequence of SEQ ID NO: 3. 3 . A polynucleotide comprising a nucleotide sequence encoding the modified polypeptide of claim 1 . 4 . A vector comprising the polynucleotide of claim 3 . 5 . A microorganism producing an L-amino acid, comprising the modified polypeptide of claim 1 , a polynucleotide comprising a nucleotide sequence encoding the modified polypeptide, or a vector comprising the polynucleotide. 6 . The microorganism of claim 5 , wherein the L-amino acid is selected from the group consisting of leucine, lysine, valine, isoleucine, and O-acetyl homoserine, and combinations thereof. 7 . The microorganism of claim 5 , wherein the microorganism is a microorganism of the genus Corynebacterium. 8 . The microorganism of claim 7 , wherein the microorganism of the genus Corynebacterium is Corynebacterium glutamicum. 9 . A method for producing an L-amino acid, comprising: culturing a microorganism in a medium to thereby produce the L-amino acid, wherein the microorganism comprises the modified polypeptide of claim 1 , a polynucleotide comprising a nucleotide sequence encoding the modified polypeptide, or a vector comprising the polynucleotide. 10 . The method of claim 9 , wherein the method further comprises recovering the L-amino acid from the cultured medium or microorganism. 11 . The method of claim 10 , wherein the L-amino acid is selected from the group consisting of leucine, lysine, valine, isoleucine, and O-acetyl homoserine, and combinations thereof.
Assignees
Inventors
Classifications
- C12Y203/03003Primary
Citrate (Re)-synthase (2.3.3.3) · CPC title
Alanine; Leucine; Isoleucine; Serine; Homoserine · CPC title
for Corynebacterium; for Brevibacterium · CPC title
Corynebacterium · CPC title
Citrate (Si)-synthase (2.3.3.1) · CPC title
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Frequently asked questions
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- What does patent US12522808B2 cover?
- The present disclosure relates to a modified polypeptide with attenuated activity of citrate synthase, a microorganism producing leucine comprising the modified polypeptide, and a method for producing an L-amino acid using the microorganism.
- Who is the assignee on this patent?
- Cj Cheiljedang Corp, Cj Chieljedang Corp
- What technology area does this patent fall under?
- Primary CPC classification C12Y203/03003. Mapped technology areas include Chemistry & Metallurgy.
- When was this patent published?
- Publication date Tue Jan 13 2026 00:00:00 GMT+0000 (Coordinated Universal Time) (B2). Legal status and post-grant events are not shown on this page.
- What related patents are in patentsdb?
- We list 3 related publications on this page (citations in our corpus or others sharing the same primary CPC).