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

نویسندگان

چکیده

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 used as electron acceptor, generating hydrogen peroxide. LAAO can be detect for production peroxide an agent or antimicrobial agent, and enantiopure amino from racemates. In work, we characterised previously reported bacterium Pseudoalteromonas luteoviolacea. The substrate scope kinetic properties were determined, thermostability was evaluated. Additionally, elucidated crystal structure bacterial LAAO, enabling us test role site residues concerning function in catalysis. obtained insights ease expression thermostable provides solid basis development engineered variants tuned biosensing and/or biocatalysis.

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ژورنال

عنوان ژورنال: Catalysts

سال: 2021

ISSN: ['2073-4344']

DOI: https://doi.org/10.3390/catal11111309