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
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

76-83

Informations de copyright

Copyright © 2018. Published by Elsevier Ltd.

Auteurs

Yasuhisa Asano (Y)

Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, 5180 Kurokawa, mizu, Toyama 939-0398, Japan. Electronic address: asano@pu-toyama.ac.jp.

Kazuyuki Yasukawa (K)

Toyama Institute of Health, 17-1 Nakataikoyama, Imizu, Toyama 939-0363, Japan.

Articles similaires

A molecular mechanism for bright color variation in parrots.

Roberto Arbore, Soraia Barbosa, Jindich Brejcha et al.
1.00
Animals Feathers Pigmentation Parrots Aldehyde Dehydrogenase

Mutational analysis of Phanerochaete chrysosporium´s purine transporter.

Mariana Barraco-Vega, Manuel Sanguinetti, Gabriela da Rosa et al.
1.00
Phanerochaete Fungal Proteins Purines Aspergillus nidulans DNA Mutational Analysis
Osteosarcoma Animals Glutathione Oxidation-Reduction Mice

Aminoacid functionalised magnetite nanoparticles Fe

Spoială Angela, Motelica Ludmila, Ilie Cornelia-Ioana et al.
1.00
Magnetite Nanoparticles Tryptophan Biocompatible Materials Microbial Sensitivity Tests Humans

Classifications MeSH