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
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

Références

Proteins. 1999 May 15;35(3):307-12
pubmed: 10328265
Arch Biochem Biophys. 1990 Apr;278(1):125-30
pubmed: 2157358
J Biol Chem. 2009 Mar 13;284(11):6610-9
pubmed: 19136717
Anal Biochem. 1990 Nov 15;191(1):110-8
pubmed: 2077933
Curr Pharm Des. 2013;19(14):2637-48
pubmed: 23116401
J Mol Biol. 2019 Jul 12;431(15):2762-2776
pubmed: 31132361
Biochim Biophys Acta. 2014 Dec;1844(12):2086-95
pubmed: 25135855
Nucleic Acids Res. 2016 Jul 8;44(W1):W344-50
pubmed: 27166375
Molecules. 2018 Jan 06;23(1):
pubmed: 29316637
J Mol Biol. 2010 Jul 9;400(2):218-30
pubmed: 20471397
Int J Mol Sci. 2019 Oct 14;20(20):
pubmed: 31614972
Front Chem. 2015 Apr 22;3:30
pubmed: 25954742
FEBS J. 2011 Nov;278(22):4434-49
pubmed: 21951714
Int J Biol Macromol. 2019 Oct 1;138:986-995
pubmed: 31351152
Protein Expr Purif. 2007 Mar;52(1):175-81
pubmed: 17049878
Biochim Biophys Acta. 2015 Aug;1854(8):897-906
pubmed: 25801930
Curr Opin Chem Biol. 2007 Apr;11(2):195-202
pubmed: 17275397
J Mol Biol. 2009 Jun 5;389(2):388-400
pubmed: 19375431
Sci Rep. 2017 Aug 8;7(1):7609
pubmed: 28790457
Anal Biochem. 1993 Feb 15;209(1):32-44
pubmed: 8465960
Proteins. 2003 Sep 1;52(4):633-5
pubmed: 12910462
Biochemistry. 2013 May 28;52(21):3615-7
pubmed: 23663086
J Mol Biol. 2010 May 21;398(5):641-6
pubmed: 20359485
Sci Rep. 2017 Mar 24;7(1):404
pubmed: 28341845
J Enzyme Inhib Med Chem. 2018 Dec;33(1):842-849
pubmed: 29693467
Biochim Biophys Acta. 2013 Mar;1834(3):665-76
pubmed: 23291469
Sci Rep. 2017 Aug 4;7(1):7281
pubmed: 28779158
Biochem Biophys Res Commun. 2015 Sep 25;465(3):443-9
pubmed: 26277395
Int J Mol Sci. 2012 Dec 11;13(12):16880-98
pubmed: 23443125
Mitochondrion. 2010 Apr;10(3):263-73
pubmed: 20060505
BMC Microbiol. 2008 Sep 23;8:160
pubmed: 18811972
Acta Crystallogr D Biol Crystallogr. 2015 Dec 1;71(Pt 12):2526-42
pubmed: 26627660
Structure. 2003 Mar;11(3):265-73
pubmed: 12623014
J Bacteriol. 2002 Aug;184(16):4555-72
pubmed: 12142426
Biophys J. 2018 Sep 18;115(6):988-995
pubmed: 30177440
FEBS J. 2011 Aug;278(15):2625-34
pubmed: 21635694
Int J Mol Sci. 2019 Dec 09;20(24):
pubmed: 31835305
J Enzyme Inhib Med Chem. 2018 Dec;33(1):241-254
pubmed: 29258359
Anal Biochem. 1989 Nov 1;182(2):319-26
pubmed: 2610349
Int J Mol Sci. 2012 Nov 08;13(11):14492-517
pubmed: 23203077

Auteurs

Ana Serrano (A)

Department of Biochemistry and Molecular and Cellular Biology, Faculty of Sciences, and Institute of Biocomputation and Physics of Complex Systems (Joint Units: BIFI-IQFR and GBsC-CSIC), University of Zaragoza, E-50009 Zaragoza, Spain.
Centro de Investigaciones Biológicas Margarita Salas, CSIC, Ramiro de Maeztu 9, E-28040 Madrid, Spain.

Sonia Arilla-Luna (S)

Department of Biochemistry and Molecular and Cellular Biology, Faculty of Sciences, and Institute of Biocomputation and Physics of Complex Systems (Joint Units: BIFI-IQFR and GBsC-CSIC), University of Zaragoza, E-50009 Zaragoza, Spain.

Milagros Medina (M)

Centro de Investigaciones Biológicas Margarita Salas, CSIC, Ramiro de Maeztu 9, E-28040 Madrid, Spain.

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Classifications MeSH