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Article

Through virtual saturation mutagenesis and rational design for superior substrate conversion in engineered d-amino acid oxidase.

Biotechnology journal - 1 Jul 2024

Tang Heng, Zhu Hong-Li, Zhao Jin-Qiao, Wang Liu-Yu, Xue Ya-Ping, Zheng Yu-Guo

Abstract excerpt

The d-amino acid oxidase (DAAO) is pivotal in obtaining optically pure l-glufosinate (l-PPT) by converting d-glufosinate (d-PPT) to its deamination product. We screened and designed a Rasamsonia emersonii DAAO (ReDAAO), making it more suitable for oxidizing d-PPT. Using Caver 3.0, we delineated three substrate binding pockets and, via alanine scanning, identified nearby key residues. Pinpointing key residues...

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Aminobutyrates
Binding Sites
Models, Molecular
Mutagenesis
Mutagenesis, Site-Directed

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Engineering

Substrate Specificity

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PMID: 39014925
DOI: 10.1002/biot.202400287

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

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