Phosphoenolpyruvate carboxykinase mutant and application thereof in production of lysine

By introducing a specific mutation into the phosphoenolpyruvate carboxylkinase of Corynebacterium glutamicum, the problem of insufficient oxaloacetic acid replenishment was solved, the fermentation production efficiency of lysine was improved, and a significant yield increase was achieved.

WO2026114008A1 Publication Date: 2026-06-04MEIHUA BIOTECH LANGFANG CO LTD
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Patent Information

Application Number
PCT/CN2025/135487
Authority / Receiving Office
WO · WO
Patent Type
Applications
Current Assignee / Owner
Priority Date
2024-11-28
Filing Date
2025-11-17
Publication Date
2026-06-04

AI Technical Summary

Technical Problem

In the existing technology, the fermentation production efficiency of L-lysine needs to be improved, especially when using Corynebacterium glutamicum as a strain, the insufficient oxaloacetic acid feedback reaction leads to low lysine synthesis efficiency.

Method used

By introducing a specific mutation into the phosphoenolpyruvate carboxykinase of Corynebacterium glutamicum, specifically by changing the amino acid at position 377 from proline to serine, a phosphoenolpyruvate carboxykinase mutant was formed, which regulated metabolic balance to improve the efficiency of lysine synthesis.

Benefits of technology

This study significantly improved the lysine fermentation yield and sugar-acid conversion rate of Corynebacterium glutamicum, providing a new method to enhance fermentation production efficiency.

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Abstract

The present invention relates to the technical field of microorganisms, and provides a phosphoenolpyruvate carboxykinase mutant and an application thereof in the production of lysine. Studies have found that mutating an amino acid at position 377 of phosphoenolpyruvate carboxykinase from proline to serine increases yield of lysine produced by a fermentation strain. Therefore, provided is a phosphoenolpyruvate carboxykinase mutant, wherein an amino acid sequence shown in SEQ ID NO. 7 or 9 is used as a reference sequence, and the phosphoenolpyruvate carboxykinase mutant comprises a mutation in which the amino acid at position 377 is mutated from proline to serine. The provided phosphoenolpyruvate carboxykinase mutant increases the fermentation yield of lysine and provides an effective new method for lysine production.
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