Novel tetrahydrofolate-dependent d-serine dehydratase activity of serine hydroxymethyltransferases.
d-amino acid
d-serine
d-serine dehydratase
pyruvate
serine hydroxymethyltransferase
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
12 Sep 2023
12 Sep 2023
Historique:
revised:
12
08
2023
received:
10
06
2023
accepted:
06
09
2023
pubmed:
13
9
2023
medline:
13
9
2023
entrez:
13
9
2023
Statut:
aheadofprint
Résumé
d-Serine plays vital physiological roles in the functional regulation of the mammalian brain, where it is produced from l-serine by serine racemase and degraded by d-amino acid oxidase. In the present study, we identified a new d-serine metabolizing activity of serine hydroxymethyltransferase (SHMT) in bacteria as well as mammals. SHMT is known to catalyze the conversion of l-serine and tetrahydrofolate (THF) to glycine and 5,10-methylenetetrahydrofolate, respectively. In addition, we found that human and Escherichia coli SHMTs have d-serine dehydratase activity, which degrades d-serine to pyruvate and ammonia. We characterized this enzymatic activity along with canonical SHMT activity. Intriguingly, SHMT required THF to catalyze d-serine dehydration and did not exhibit dehydratase activity toward l-serine. Furthermore, SHMT did not use d-serine as a substrate in the canonical hydroxymethyltransferase reaction. The d-serine dehydratase activities of two isozymes of human SHMT were inhibited in the presence of a high concentration of THF, whereas that of E. coli SHMT was increased. The pH and temperature profiles of d-serine dehydratase and serine hydroxymethyltransferase activities of these three SHMTs were partially distinct. The catalytic efficiency (k
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Ito Science Foundation
Organisme : Japan Society for the Promotion of Science
ID : 21K05348
Informations de copyright
© 2023 Federation of European Biochemical Societies.
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