d-Aspartate N-methyltransferase catalyzes biosynthesis of N-methyl-d-aspartate (NMDA), a well-known selective agonist of the NMDA receptor, in mice.


Journal

Biochimica et biophysica acta. Proteins and proteomics
ISSN: 1878-1454
Titre abrégé: Biochim Biophys Acta Proteins Proteom
Pays: Netherlands
ID NLM: 101731734

Informations de publication

Date de publication:
12 2020
Historique:
received: 28 02 2020
revised: 15 07 2020
accepted: 03 08 2020
pubmed: 28 8 2020
medline: 15 12 2020
entrez: 28 8 2020
Statut: ppublish

Résumé

N-Methyl-d-aspartate (NMDA), which is a selective agonist for the NMDA receptor, has recently been shown to be present in various biological tissues. In mammals, the activity of d-aspartate N-methyltransferase (DDNMT), which produces NMDA from d-aspartate, has been detected only in homogenates prepared from rat tissues. Moreover, the enzymatic properties of DDNMT have been poorly studied and its molecular entity has not yet been identified. In this report, we show for the first time that the activity of DDNMT is present in mouse tissues and succeed in obtaining a partially purified enzyme preparation from a mouse tissue homogenate with a purification fold of 1900 or more, and have characterized the enzymatic activity of this preparation. The results indicate that DDNMT, which is highly specific for d-aspartate and is S-adenosyl-l-methionine-dependent, is a novel enzyme that clearly differs from the known methylamine-glutamate N-methyltransferase (EC 2.1.1.21) and glycine N-methyltransferase (EC 2.1.1.20).

Identifiants

pubmed: 32853768
pii: S1570-9639(20)30174-6
doi: 10.1016/j.bbapap.2020.140527
pii:
doi:

Substances chimiques

Receptors, N-Methyl-D-Aspartate 0
Recombinant Proteins 0
N-Methylaspartate 6384-92-5
Methyltransferases EC 2.1.1.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

140527

Informations de copyright

Copyright © 2020 Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Competing Interest The authors have no potential conflict of interest.

Auteurs

Kimihiko Shibata (K)

Department of Bioengineering, Nagaoka University of Technology, 1603-1, Kamitomioka-machi, Nagaoka, Niigata 940-2188, Japan; Department of Applied Chemistry and Biochemistry, National Institute of Technology (KOSEN), Fukushima College, 30 Nagao, Kamiarakawa, Taira, Iwaki, Fukushima, 970-8034, Japan. Electronic address: shibata@fukushima-nct.ac.jp.

Daiki Imanishi (D)

Department of Bioengineering, Nagaoka University of Technology, 1603-1, Kamitomioka-machi, Nagaoka, Niigata 940-2188, Japan; Department of Applied Chemistry and Biochemistry, National Institute of Technology (KOSEN), Fukushima College, 30 Nagao, Kamiarakawa, Taira, Iwaki, Fukushima, 970-8034, Japan.

Katsumasa Abe (K)

Department of Bioengineering, Nagaoka University of Technology, 1603-1, Kamitomioka-machi, Nagaoka, Niigata 940-2188, Japan.

Masataka Suzuki (M)

Department of Applied Chemistry and Biochemistry, National Institute of Technology (KOSEN), Fukushima College, 30 Nagao, Kamiarakawa, Taira, Iwaki, Fukushima, 970-8034, Japan.

Shouji Takahashi (S)

Department of Bioengineering, Nagaoka University of Technology, 1603-1, Kamitomioka-machi, Nagaoka, Niigata 940-2188, Japan.

Yoshio Kera (Y)

Department of Bioengineering, Nagaoka University of Technology, 1603-1, Kamitomioka-machi, Nagaoka, Niigata 940-2188, Japan.

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