D-Aspartate oxidase: distribution, functions, properties, and biotechnological applications.


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
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

2883-2895

Subventions

Organisme : Grant-in-Aid for Scientific Research (C) from the Japan Society for the Promotion of Science
ID : 19K05765

Auteurs

Shouji Takahashi (S)

Department of Bioengineering, Nagaoka University of Technology, Nagaoka, Niigata, 940-2188, Japan. shoutaka@vos.nagaokaut.ac.jp.

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Classifications MeSH