Kinetic and structural details of urease inactivation by thiuram disulphides.
Enzyme inactivation
Nickel
Protein X-ray crystallography
Quantum mechanical calculations
Thiuram disulphides
Urease
Journal
Journal of inorganic biochemistry
ISSN: 1873-3344
Titre abrégé: J Inorg Biochem
Pays: United States
ID NLM: 7905788
Informations de publication
Date de publication:
Jan 2024
Jan 2024
Historique:
received:
08
08
2023
revised:
21
09
2023
accepted:
07
10
2023
medline:
7
12
2023
pubmed:
26
10
2023
entrez:
25
10
2023
Statut:
ppublish
Résumé
This paper reports on the molecular details of the reactivity of urease, a nickel-dependent enzyme that catalyses the last step of organic nitrogen mineralization, with thiuram disulphides, a class of molecules known to inactivate the enzyme with high efficacy but for which the mechanism of action had not been yet established. IC
Identifiants
pubmed: 37879152
pii: S0162-0134(23)00280-5
doi: 10.1016/j.jinorgbio.2023.112398
pii:
doi:
Substances chimiques
Thiram
0D771IS0FH
Nickel
7OV03QG267
Urease
EC 3.5.1.5
Cysteine
K848JZ4886
Protons
0
Disulfiram
TR3MLJ1UAI
Urea
8W8T17847W
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
112398Informations de copyright
Copyright © 2023. Published by Elsevier Inc.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.