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...
Saved in:
Main Authors: | Simone Savino, J. Daniël-Moráh Meijer, Henriëtte J. Rozeboom, Hugo L. van Beek, Marco W. Fraaije |
---|---|
Format: | article |
Language: | EN |
Published: |
MDPI AG
2021
|
Subjects: | |
Online Access: | https://doaj.org/article/b392d89215da4e66bbe3cfe598dc20d3 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
SPECTROSCOPIC PROPERTIES OF HYDROPHOBIC FLAVIN ESTERS.: A ONE AND TWO-DIMENSIONAL ¹H-NMR AND 13C-NMR STUDY
by: Edwards,A.M., et al.
Published: (2000) -
L-Lysine α-Oxidase: Enzyme with Anticancer Properties
by: Elena V. Lukasheva, et al.
Published: (2021) -
Biocatalytic oxidative kinetic resolution of (±)-4-(chlorophenyl)phenylmethanol by Nocardia corallina B-276
by: Ramírez,Mario A., et al.
Published: (2008) -
Biotechnological applications of archaeal enzymes from extreme environments
by: Cabrera,Ma. Ángeles, et al.
Published: (2018) - Journal of amino acids