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Kinetic and structural properties of a robust bacterial L-amino acid oxidase

DOI: 10.3390/catal11111309 DOI Help

Authors: Simone Savino (GECCO Biotech; University of Groningen) , J. Daniël-Moráh Meijer (University of Groningen) , Henriëtte J. Rozeboom (University of Groningen) , Hugo L. Van Beek (GECCO Biotech) , Marco W. Fraaije (University of Groningen)
Co-authored by industrial partner: Yes

Type: Journal Paper
Journal: Catalysts , VOL 11

State: Published (Approved)
Published: November 2021
Diamond Proposal Number(s): 19800

Open Access Open Access

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.

Journal Keywords: flavin-dependent oxidase; L-amino acids; deracemisation; biocatalysis; crystal structure

Diamond Keywords: Bacteria; Enzymes

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I24-Microfocus Macromolecular Crystallography

Added On: 10/11/2021 08:20

Discipline Tags:

Catalysis Life Sciences & Biotech Structural biology Chemistry Biochemistry

Technical Tags:

Diffraction Macromolecular Crystallography (MX)