Back to Search
Start Over
Kinetic and Structural Properties of a Robust Bacterial L-Amino Acid Oxidase
- Source :
- Catalysts, Vol 11, Iss 11, p 1309 (2021)
- Publication Year :
- 2021
- Publisher :
- MDPI AG, 2021.
-
Abstract
- L-Amino acid oxidase (LAAO) is a flavin adenine dinucleotide (FAD)-dependent enzyme active on most proteinogenic L-amino acids, catalysing their conversion to α-keto acids by oxidative deamination of the substrate. For this oxidation reaction, molecular oxygen is used as the electron acceptor, generating hydrogen peroxide. LAAO can be used to detect L-amino acids, for the production of hydrogen peroxide as an oxidative agent or antimicrobial agent, and for the production of enantiopure amino acids from racemates. In this work, we characterised a previously reported LAAO from the bacterium Pseudoalteromonas luteoviolacea. The substrate scope and kinetic properties of the enzyme were determined, and the thermostability was evaluated. Additionally, we elucidated the crystal structure of this bacterial LAAO, enabling us to test the role of active site residues concerning their function in catalysis. The obtained insights and ease of expression of this thermostable LAAO provides a solid basis for the development of engineered LAAO variants tuned for biosensing and/or biocatalysis.
Details
- Language :
- English
- ISSN :
- 20734344
- Volume :
- 11
- Issue :
- 11
- Database :
- Directory of Open Access Journals
- Journal :
- Catalysts
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.b392d89215da4e66bbe3cfe598dc20d3
- Document Type :
- article
- Full Text :
- https://doi.org/10.3390/catal11111309