D-Aspartate oxidase: distribution, functions, properties, and biotechnological applications.
Acidic D-amino acids
Applications
D-aspartate oxidase
Flavoenzyme
Oxidoreductase
Journal
Applied microbiology and biotechnology
ISSN: 1432-0614
Titre abrégé: Appl Microbiol Biotechnol
Pays: Germany
ID NLM: 8406612
Informations de publication
Date de publication:
Apr 2020
Apr 2020
Historique:
received:
05
01
2020
accepted:
05
02
2020
revised:
28
01
2020
pubmed:
12
2
2020
medline:
28
11
2020
entrez:
12
2
2020
Statut:
ppublish
Résumé
Recently, substantial levels of acidic D-amino acids, such as D-aspartate and D-glutamate, have been identified in many organisms, from bacteria to mammals, suggesting that acidic D-amino acids have multiple physiological significances. Although acidic D-amino acids found in animals primarily originate from foodstuffs and/or bacteria, the D-aspartate-synthesizing enzyme aspartate racemase is identified in various animals. In eukaryotic organisms, acidic D-amino acids are primarily degraded by the flavoenzyme D-aspartate oxidase (DDO). DDO is found in multiple eukaryotic organisms and may play important roles in acidic D-amino acid utilization, elimination, and intracellular level regulation. Moreover, owing to its perfect enantioselectivity and stereoselectivity, DDO may be a valuable tool in several biotechnological applications, including the identification and quantification of acidic D-amino acids. In this mini-review, previous DDO reports are summarized and the potential bioengineering and biotechnological applications of DDO are discussed. Key Points ・Occurrence and distribution ofd-aspartate oxidase. ・Fundamental properties of d -aspartate oxidase of various eukaryotic organisms. ・Biotechnological applications and potential engineering ofd-aspartate oxidase.
Identifiants
pubmed: 32043187
doi: 10.1007/s00253-020-10439-9
pii: 10.1007/s00253-020-10439-9
doi:
Substances chimiques
Amino Acids, Acidic
0
Recombinant Proteins
0
D-Aspartate Oxidase
EC 1.4.3.1
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
2883-2895Subventions
Organisme : Grant-in-Aid for Scientific Research (C) from the Japan Society for the Promotion of Science
ID : 19K05765