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In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

Published on: March 25, 2020

Combinatorial engineering of dextransucrase specificity.

Romain Irague¹, Laurence Tarquis, Isabelle André

¹Université de Toulouse; INSA, UPS, INP, LISBP, Toulouse, France ; CNRS, UMR5504, Toulouse, France ; INRA, UMR792 Ingénierie des Systèmes Biologiques et des Procédés, Toulouse, France.

|November 9, 2013

Summary

This summary is machine-generated.

Combinatorial engineering of dextransucrase DSR-S identified key amino acids, including the DYVHT peptide, that control α-glucan linkage specificity. This work generates novel variants with tailored α(1→3) linkage proportions for potential applications.

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Area of Science:

Enzymology
Protein Engineering
Carbohydrate Chemistry

Background:

Dextransucrase DSR-S from Leuconostoc mesenteroides NRRL B-512F synthesizes α-glucans.
Understanding enzyme structure-function relationships is crucial for modifying specificity.

Purpose of the Study:

Investigate structure-linkage specificity of DSR-S.
Generate DSR-S variants with altered α-glucan linkage specificity.

Main Methods:

Combinatorial engineering and saturation mutagenesis.
Screening of enzyme variant libraries.
Biochemical characterization and molecular modeling.

Main Results:

Isolated 81 DSR-S variants with α(1→3) linkage proportions from 3% to 20%.
Identified the peptide (460)DYVHT(464) and residue S512 as critical for DSR-S regiospecificity.
Determined the role of this peptide in defining the +2 subsite topology.

Conclusions:

The peptide DYVHT and residue S512 are key determinants of DSR-S linkage specificity.
Combinatorial engineering is effective for tailoring dextransucrase activity.
Findings provide insights into glycoside hydrolase family 70 enzyme specificity.