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Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase

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Published on: November 23, 2016

Active-site engineering of ω-transaminase from Ochrobactrum anthropi for preparation of L-2-aminobutyric acid.

Zhiwei Zhang¹, Yang Liu¹, Jing Zhao¹

¹State Key Laboratory of Biocatalysis and Enzyme Engineering, Hubei Collaborative Innovation Center for Green Transformation of Bio-Resources, Hubei Key Laboratory of Industrial Biotechnology, College of Life Sciences, Hubei University, 368 Youyi Road, Wuchang, Wuhan, 430062, China.

BMC Biotechnology

|September 26, 2021

Summary

This summary is machine-generated.

Protein engineering of Ochrobactrum anthropi ω-transaminase (OATA) enhanced its activity towards α-ketobutyric acid. Engineered OATA efficiently produced L-2-aminobutyric acid (L-ABA) from L-threonine with high purity and enantiomeric excess.

Keywords:

L-2-aminobutyric acid L57C/M419I variant Molecular docking Saturation mutagenesis ω-transaminase

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Published on: June 20, 2019

Area of Science:

Biocatalysis and Enzyme Engineering
Organic Chemistry
Pharmaceutical Synthesis

Background:

L-2-aminobutyric acid (L-ABA) is a crucial chiral building block for pharmaceuticals like levetiracetam and ethambutol.
Ochrobactrum anthropi ω-transaminase (OATA) is a key enzyme for synthesizing chiral amines.

Purpose of the Study:

To engineer OATA variants with enhanced catalytic activity for α-ketobutyric acid.
To improve the production of L-ABA using biocatalysis.

Main Methods:

Protein engineering through saturation mutagenesis of OATA based on docking models.
Identification and characterization of high-activity variants, including double substitutions.
Coupled enzymatic reaction system using engineered OATA for L-ABA synthesis.

Main Results:

Specific amino acid substitutions (L57C, M419I, A230S) significantly increased OATA activity.
A double mutant (L57C/M419I) exhibited a 3.2-fold increase in catalytic efficiency.
The engineered OATA achieved 94% conversion of L-threonine to L-ABA with >99% enantiomeric excess and 75% purity.

Conclusions:

Engineered OATA provides an efficient biocatalytic route for L-ABA production.
This study lays the groundwork for further enzyme engineering of transaminases for chiral amine synthesis.