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
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

51-74

Informations de copyright

Copyright © 2024. Published by Elsevier Inc.

Auteurs

Thiago M Pasin (TM)

Department of Chemistry, University of Texas at San Antonio, San Antonio, TX, United States.

Kathleen M Meneely (KM)

Department of Chemistry, University of Texas at San Antonio, San Antonio, TX, United States.

Deegan M Ruiz (DM)

Department of Chemistry, University of Texas at San Antonio, San Antonio, TX, United States.

Audrey L Lamb (AL)

Department of Chemistry, University of Texas at San Antonio, San Antonio, TX, United States. Electronic address: audrey.lamb@utsa.edu.

Articles similaires

Anthraquinones Kinetics Water Purification Adsorption Thermodynamics
1.00
Humans Pyrophosphatases Protein Conformation Molecular Dynamics Simulation Kinetics
Aluminum Carbon Quantum Dots Spectrometry, Fluorescence Limit of Detection

Classifications MeSH