Identification and development of amino acid oxidases.
Journal
Current opinion in chemical biology
ISSN: 1879-0402
Titre abrégé: Curr Opin Chem Biol
Pays: England
ID NLM: 9811312
Informations de publication
Date de publication:
04 2019
04 2019
Historique:
received:
26
09
2018
revised:
16
10
2018
accepted:
22
10
2018
pubmed:
19
11
2018
medline:
18
12
2019
entrez:
19
11
2018
Statut:
ppublish
Résumé
Amino acid oxidases are an important class of enzymes that mostly participate in the oxidation of amino acids using FAD as a cofactor. Many of them function in the catabolism of amino acids with wider substrate specificities. On the other hand, based on the recent, successful use of the enzymes for diagnoses with new cofactor and mechanism, highly selective enzymes have been screened from Nature, and many new enzymes have been discovered and further characterized by X-ray crystallography. As a result of the screening for amino acid oxidases with biosynthetic or antibiotic functions, l-Trp oxidase, l-Lys oxidases, and Gly oxidase have been found. The pyridoxal phosphate-dependent l-Arg oxidase has the intriguing new activity of hydroxylating unactivated CC bonds. A new amine oxidase was created by the protein engineering of d-amino acid oxidase. Recent developments in the characterization of amino acid oxidases and their applications are summarized.
Identifiants
pubmed: 30448541
pii: S1367-5931(18)30144-3
doi: 10.1016/j.cbpa.2018.10.020
pii:
doi:
Substances chimiques
Amino Acids
0
D-Amino-Acid Oxidase
EC 1.4.3.3
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
76-83Informations de copyright
Copyright © 2018. Published by Elsevier Ltd.