Substrate-Dependent Mobile Loop Conformational Changes in Alkanesulfonate Monooxygenase from Accelerated Molecular Dynamics.
Alkanesulfonic Acids
/ chemistry
Catalytic Domain
Escherichia coli
/ enzymology
Escherichia coli Proteins
/ chemistry
Flavins
/ chemistry
Kinetics
Mixed Function Oxygenases
/ chemistry
Models, Chemical
Molecular Dynamics Simulation
Oxidation-Reduction
Protein Binding
Protein Conformation
Substrate Specificity
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
29 09 2020
29 09 2020
Historique:
pubmed:
4
9
2020
medline:
31
3
2021
entrez:
4
9
2020
Statut:
ppublish
Résumé
Substrate-induced conformational changes present in alkanesulfonate monooxygenase (SsuD) are crucial to catalysis and lead to distinct interactions between a dynamic loop region and the active site. Accelerated molecular dynamics (aMD) simulations have been carried out to examine this potential correlation by studying wild-type SsuD and variant enzymes bound with different combinations of reduced flavin (FMNH
Identifiants
pubmed: 32881481
doi: 10.1021/acs.biochem.0c00633
doi:
Substances chimiques
Alkanesulfonic Acids
0
C4a-hydroperoxyflavin
0
Escherichia coli Proteins
0
Flavins
0
1-octanesulfonic acid
DU4821I15A
Mixed Function Oxygenases
EC 1.-
SsuD protein, E coli
EC 1.14.14.5
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