Kinetic and Structural Properties of a Robust Bacterial L-Amino Acid Oxidase

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, gener...

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Autores principales:	Simone Savino, J. Daniël-Moráh Meijer, Henriëtte J. Rozeboom, Hugo L. van Beek, Marco W. Fraaije
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	flavin-dependent oxidase L-amino acids deracemisation biocatalysis crystal structure Chemical technology TP1-1185 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/b392d89215da4e66bbe3cfe598dc20d3
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spelling	oai:doaj.org-article:b392d89215da4e66bbe3cfe598dc20d32021-11-25T17:05:41ZKinetic and Structural Properties of a Robust Bacterial L-Amino Acid Oxidase10.3390/catal111113092073-4344https://doaj.org/article/b392d89215da4e66bbe3cfe598dc20d32021-10-01T00:00:00Zhttps://www.mdpi.com/2073-4344/11/11/1309https://doaj.org/toc/2073-4344L-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 <i>Pseudoalteromonas luteoviolacea</i>. 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.Simone SavinoJ. Daniël-Moráh MeijerHenriëtte J. RozeboomHugo L. van BeekMarco W. FraaijeMDPI AGarticleflavin-dependent oxidaseL-amino acidsderacemisationbiocatalysiscrystal structureChemical technologyTP1-1185ChemistryQD1-999ENCatalysts, Vol 11, Iss 1309, p 1309 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	flavin-dependent oxidase L-amino acids deracemisation biocatalysis crystal structure Chemical technology TP1-1185 Chemistry QD1-999
spellingShingle	flavin-dependent oxidase L-amino acids deracemisation biocatalysis crystal structure Chemical technology TP1-1185 Chemistry QD1-999 Simone Savino J. Daniël-Moráh Meijer Henriëtte J. Rozeboom Hugo L. van Beek Marco W. Fraaije Kinetic and Structural Properties of a Robust Bacterial L-Amino Acid Oxidase
description	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 <i>Pseudoalteromonas luteoviolacea</i>. 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.
format	article
author	Simone Savino J. Daniël-Moráh Meijer Henriëtte J. Rozeboom Hugo L. van Beek Marco W. Fraaije
author_facet	Simone Savino J. Daniël-Moráh Meijer Henriëtte J. Rozeboom Hugo L. van Beek Marco W. Fraaije
author_sort	Simone Savino
title	Kinetic and Structural Properties of a Robust Bacterial L-Amino Acid Oxidase
title_short	Kinetic and Structural Properties of a Robust Bacterial L-Amino Acid Oxidase
title_full	Kinetic and Structural Properties of a Robust Bacterial L-Amino Acid Oxidase
title_fullStr	Kinetic and Structural Properties of a Robust Bacterial L-Amino Acid Oxidase
title_full_unstemmed	Kinetic and Structural Properties of a Robust Bacterial L-Amino Acid Oxidase
title_sort	kinetic and structural properties of a robust bacterial l-amino acid oxidase
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/b392d89215da4e66bbe3cfe598dc20d3
work_keys_str_mv	AT simonesavino kineticandstructuralpropertiesofarobustbacteriallaminoacidoxidase AT jdanielmorahmeijer kineticandstructuralpropertiesofarobustbacteriallaminoacidoxidase AT henriettejrozeboom kineticandstructuralpropertiesofarobustbacteriallaminoacidoxidase AT hugolvanbeek kineticandstructuralpropertiesofarobustbacteriallaminoacidoxidase AT marcowfraaije kineticandstructuralpropertiesofarobustbacteriallaminoacidoxidase
_version_	1718412735024201728

Kinetic and Structural Properties of a Robust Bacterial L-Amino Acid Oxidase

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