O-Phosphoserine Sulfhydrylase Variant for Higher L-Cysteine Yield

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Solution Overview

Problem

Existing methods for producing L-cysteine, particularly through the conversion of O-phosphoserine using wild-type O-phosphoserine sulfhydrylase, result in suboptimal yields.

Innovation Solution

A variant of O-phosphoserine sulfhydrylase is developed by deleting 0 to 7 amino acid residues from the C-terminus and substituting the amino acid at position 77 with alanine, enhancing the enzyme's activity.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Productivity

If wild-type O-phosphoserine sulfhydrylase is used for converting O-phosphoserine to L-cysteine, then the production process is simple, but the yield of L-cysteine is suboptimal

Engineering Contradiction:

ImproveL-cysteine yieldVSAvoidenzyme structure complexity

Core Design Contradiction:

ProductivityVSDevice complexity

Solution Approach 1:

The patent applies parameter changes by modifying specific amino acid residues in the O-phosphoserine sulfhydrylase enzyme structure. The C-terminal truncation (removing 0-7 amino acids) and substitution at position 77 (changing to alanine or serine) are systematic parameter modifications that enhance catalytic activity and L-cysteine yield while maintaining the enzyme's core functionality

Inventive Principle:

Principle #35Parameter changes

Solution Approach 2:

The patent implements local quality by making targeted modifications at specific locations (C-terminus and position 77) rather than global changes. These localized structural alterations optimize the enzyme's active site or regulatory regions to improve catalytic efficiency for L-cysteine production without affecting the entire enzyme structure

Inventive Principle:

Principle #3Local quality

2Productivity

If O-phosphoserine is produced in excessive amounts to achieve high cysteine yield, then the cysteine production increases, but the consumption of precursor material increases

Engineering Contradiction:

Improvecysteine production yieldVSAvoidO-phosphoserine consumption

Core Design Contradiction:

ProductivityVSQuantity of substance

Solution Approach 1:

The modified enzyme with C-terminal truncation and position 77 substitution exhibits enhanced catalytic efficiency, allowing effective conversion of O-phosphoserine to cysteine. This reduces the need to produce excessive O-phosphoserine intermediate, thereby improving overall yield while reducing precursor consumption

Inventive Principle:

Principle #35Parameter changes

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 O-phosphoserine sulfhydrylase variant significantly increases the yield of L-cysteine production compared to wild-type enzymes.

Implementation Method 1

converting O-phosphoserine into L-cysteine by reacting O-phosphoserine with a sulfide under the catalytic action of O-phosphoserine sulfhydrylase

Methodology Applied

Scientific EffectEnzyme catalysis: Enzyme

Data Source

PatentEP4696774A1O-phosphoserine sulfhydrylase variant and method for producing cysteine using same

Publication Date: 2026.02.18 CJ CHEILJEDANG CORP

Figure 1

AI summary

The present disclosure relates to an O-phosphoserine sulfhydrylase variant and a method for producing cysteine using the same.