Branched-Chain Amino Acid Permease Variant for L-Valine Production
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Solution Overview
Problem
Current methods for increasing L-valine production in Corynebacterium glutamicum are not sufficient to meet the growing demand, as they rely on increasing expression of biosynthesis genes or removing unnecessary genes, which are not effective enough.
Innovation Solution
A branched-chain amino acid permease variant with an amino acid sequence represented by SEQ ID NO: 1, where alanine at position 112 is substituted with threonine, is introduced into Corynebacterium glutamicum, enhancing its L-valine producing ability.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Productivity
If expression of biosynthesis genes is increased or unnecessary genes are removed, then L-valine production is improved, but the production capacity is not sufficient to meet growing demand
Solution Approach 1:
The invention applies parameter changes by modifying the amino acid sequence of the branched-chain amino acid permease protein. Specifically, alanine at position 112 is substituted with threonine, which changes the physical and chemical properties of the protein and enhances its function in L-valine transport and production, thereby resolving the insufficiency of current production methods
Solution Approach 2:
The invention applies local quality by making a targeted local modification to the permease protein structure. Instead of globally altering the entire protein or using general metabolic engineering approaches, a specific amino acid residue (position 112) is modified to threonine, which locally enhances the protein's function and consequently improves overall L-valine production capacity
Data Source
AI summary
The present disclosure relates to a novel branched-chain amino acid permease variant, a Corynebacterium glutamicum strain comprising the variant, and a method for producing L-valine using the strain.