The metabolite repair enzyme Nit1 is a dual-targeted amidase that disposes of damaged glutathione in
Nit1 proteins
glutathione
glutathione damage
metabolite damage
metabolite repair
Journal
The Biochemical journal
ISSN: 1470-8728
Titre abrégé: Biochem J
Pays: England
ID NLM: 2984726R
Informations de publication
Date de publication:
19 02 2019
19 02 2019
Historique:
received:
09
12
2018
revised:
16
01
2019
accepted:
28
01
2019
pubmed:
30
1
2019
medline:
19
12
2019
entrez:
30
1
2019
Statut:
epublish
Résumé
The tripeptide glutathione (GSH) is implicated in various crucial physiological processes including redox buffering and protection against heavy metal toxicity. GSH is abundant in plants, with reported intracellular concentrations typically in the 1-10 mM range. Various aminotransferases can inadvertently transaminate the amino group of the γ-glutamyl moiety of GSH to produce deaminated glutathione (dGSH), a metabolite damage product. It was recently reported that an amidase known as Nit1 participates in dGSH breakdown in mammals and yeast. Plants have a hitherto uncharacterized homolog of the Nit1 amidase. We show that recombinant
Identifiants
pubmed: 30692244
pii: BCJ20180931
doi: 10.1042/BCJ20180931
doi:
Substances chimiques
Arabidopsis Proteins
0
Amidohydrolases
EC 3.5.-
amidase
EC 3.5.1.4
Aminohydrolases
EC 3.5.4.-
nitrilase
EC 3.5.5.1
Glutathione
GAN16C9B8O
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
683-697Commentaires et corrections
Type : CommentIn
Informations de copyright
© 2019 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.