A continuous fluorescence assay to measure nicotianamine synthase activity.
Adenine deaminase
Amplex red
Fluorescence
Methylthioadenosine
Nicotianamine
Nucleosidase
Opine metallophore
Polyamine
S-adenosylmethionine
Synthase
Journal
Methods in enzymology
ISSN: 1557-7988
Titre abrégé: Methods Enzymol
Pays: United States
ID NLM: 0212271
Informations de publication
Date de publication:
2024
2024
Historique:
medline:
19
8
2024
pubmed:
19
8
2024
entrez:
18
8
2024
Statut:
ppublish
Résumé
S-adenosylmethionine (SAM) is most widely known as the biological methylating agent of methyltransferases and for generation of radicals by the iron-sulfur dependent Radical SAM enzymes. SAM also serves as a substrate in biosynthetic reactions that harvest the aminobutyrate moiety of the methionine, producing methylthioadenosine as a co-product. These reactions are found in the production of polyamines such as spermine, siderophores derived from nicotianamine, and opine metallophores staphylopine and pseudopaline, among others. This procedure defines a highly sensitive, continuous fluorescence assay for the determination of steady state kinetic parameters for enzymes that generate the co-product methylthioadenosine.
Identifiants
pubmed: 39155120
pii: S0076-6879(24)00317-3
doi: 10.1016/bs.mie.2024.06.013
pii:
doi:
Substances chimiques
S-Adenosylmethionine
7LP2MPO46S
nicotianamine synthase
EC 2.5.-
Alkyl and Aryl Transferases
EC 2.5.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
51-74Informations de copyright
Copyright © 2024. Published by Elsevier Inc.