Copper-Exporting ATPase Variant for Higher L-Tryptophan Yield
Find Innovative SolutionsGenerate Solutions
Solution Overview
Problem
Existing methods for increasing L-tryptophan production in microorganisms are inefficient, necessitating the development of improved strategies to enhance production yields.
Innovation Solution
A novel copper-exporting P-type ATPase A variant, represented by SEQ ID NO: 1 with a serine substitution at position 786 to asparagine, is introduced into an Escherichia coli strain, along with a polynucleotide encoding this variant, to increase L-tryptophan production.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Productivity
If conventional methods (increasing expression of biosynthesis enzymes or removing unnecessary genes) are used to increase L-tryptophan production, then production ability is improved to some extent, but the production yield remains insufficient to meet increasing demand
Solution Approach 1:
The patent applies parameter changes by modifying a specific amino acid residue (Serine to Asparagine substitution at position 786) in the copper-exporting P-type ATPase A protein. This targeted molecular parameter change optimizes copper export function, which in turn enhances L-tryptophan production yield significantly compared to conventional genetic modification approaches
Solution Approach 2:
The patent uses a polynucleotide sequence (SEQ ID NO: 2) that encodes the modified ATPase A protein. This molecular copy carries the specific amino acid substitution (S786N) that confers enhanced copper export capability, allowing the modified protein to be produced in the host organism to achieve higher L-tryptophan yields
2Productivity
If the copper-exporting P-type ATPase A variant is introduced into Escherichia coli strain, then L-tryptophan production yield is significantly increased, but the complexity of the organism's genetic makeup is increased
Solution Approach 1:
The patent applies local quality by making a targeted modification at a specific location (position 786) within the ATPase A protein sequence. Only the amino acid at this specific position is changed from Serine to Asparagine, while the rest of the protein structure and function remain intact. This localized change optimizes copper export without requiring comprehensive genetic redesign
Solution Approach 2:
The patent segments the genetic modification into a discrete, manageable unit - a specific amino acid substitution encoded by a defined polynucleotide sequence. This segmentation allows the modification to be introduced as a distinct genetic element (SEQ ID NO: 2) that can be independently manipulated and expressed, simplifying the overall genetic engineering process
Applied Scientific Principles
This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.
Function Achieved in This Case
The modified Escherichia coli strain exhibits a higher yield of L-tryptophan production compared to unmodified microorganisms, with increased production rates ranging from 1% to 200% above baseline.
Implementation Method 1
copper-exporting P-type ATPase A variant
Data Source
AI summary
The present disclosure relates to a novel copper-exporting P-type ATPase A variant, an Escherichia coli strain comprising the variant, and a method for producing L-tryptophan using the strain.