Transition-State Interactions in a Promiscuous Enzyme: Sulfate and Phosphate Monoester Hydrolysis by Pseudomonas aeruginosa Arylsulfatase.
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
12 03 2019
12 03 2019
Historique:
pubmed:
28
2
2019
medline:
7
1
2020
entrez:
28
2
2019
Statut:
ppublish
Résumé
Pseudomonas aeruginosa arylsulfatase (PAS) hydrolyzes sulfate and, promiscuously, phosphate monoesters. Enzyme-catalyzed sulfate transfer is crucial to a wide variety of biological processes, but detailed studies of the mechanistic contributions to its catalysis are lacking. We present linear free energy relationships (LFERs) and kinetic isotope effects (KIEs) of PAS and analyses of active site mutants that suggest a key role for leaving group (LG) stabilization. In LFERs PAS
Identifiants
pubmed: 30810299
doi: 10.1021/acs.biochem.8b00996
doi:
Substances chimiques
Organophosphates
0
Organophosphorus Compounds
0
Phosphates
0
Sulfates
0
Sulfatases
EC 3.1.6.-
Arylsulfatases
EC 3.1.6.1
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1363-1378Subventions
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/I004327/1
Pays : United Kingdom