Insights into the FMNAT Active Site of FAD Synthase: Aromaticity is Essential for Flavin Binding and Catalysis.
aromatic residues
binding
eukaryotic ATP:FMN:adenylyltransferase
flavin biosynthesis
isoalloxazine
isothermal titration calorimetry
prokaryotic FAD synthase
rational mutagenesis
steady-state kinetics
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
25 May 2020
25 May 2020
Historique:
received:
01
05
2020
revised:
21
05
2020
accepted:
22
05
2020
entrez:
30
5
2020
pubmed:
30
5
2020
medline:
18
2
2021
Statut:
epublish
Résumé
The last step in the biosynthesis of flavin adenine dinucleotide (FAD) is considered a target for the design of antimicrobial drugs because it is carried out by two non-homologous proteins in eukaryotic and prokaryotic organisms. Monofunctional FMN: adenylyltransferases (FMNAT) in Eukarya and FMNAT modules of bifunctional FAD synthases (FADS) in Prokarya belong to different structural families with dissimilar chemistry and binding modes for the substrates. In this study, we analyzed the relevance of the hydrophobic environment of the flavin isoalloxazine in the FMNAT active site of
Identifiants
pubmed: 32466340
pii: ijms21103738
doi: 10.3390/ijms21103738
pmc: PMC7279473
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Dinitrocresols
0
4,6-dinitro-o-cresol
1604ZJR09T
Tyrosine
42HK56048U
Phenylalanine
47E5O17Y3R
Nucleotidyltransferases
EC 2.7.7.-
FMN adenylyltransferase
EC 2.7.7.2
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Government of Aragon-FEDER
ID : E35_20R
Organisme : Spanish Agencia Estatal de Investigación and Fondo Europeo de Desarrollo Regional
ID : BIO2016-75183-P AEI/FEDER
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