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References from The riboflavin kinase domain is essential for FMNAT catalysis: A linker-dependent regulatory mechanism in Staphylococcus aureus FAD synthetase. Local targets link to admitted publications; unresolved targets remain external evidence.
The puzzle of ligand binding to Corynebacterium ammoniagenes FAD synthetase
10.1074/jbc.m808142200 · 2009 · External reference
Role of key residues at the Flavin Mononucleotide (FMN):Adenylyltransferase catalytic site of the bifunctional riboflavin Kinase/Flavin Adenine Dinucleotide (FAD) synthetase from Corynebacterium ammoniagenes
10.3390/ijms131114492 · 2012 · External reference
The diverse roles of Flavin coenzymesNature's Most versatile thespians
10.1021/jo0703092 · 2007 · External reference
Insights into the role of F26 residue in the FMN: ATP adenylyltransferase activity of Staphylococcus aureus FAD synthetase
10.1016/j.bbapap.2022.140781 · 2022 · External reference
The FAD synthetase from the human pathogen streptococcus pneumoniae: a bifunctional enzyme exhibiting activity-dependent redox requirements
10.1038/s41598-017-07716-5 · 2017 · External reference
Kinetics and thermodynamics of the protein-ligand interactions in the riboflavin kinase activity of the FAD synthetase from Corynebacterium ammoniagenes
10.1038/s41598-017-07875-5 · 2017 · External reference
The biosynthesis of Flavin cofactors in Listeria monocytogenes
10.1016/j.jmb.2019.05.029 · 2019 · External reference
Flavokinase and FAD synthetase from Bacillus subtilis specific for reduced flavins
10.1016/s0021-9258(19)83550-0 · 1979 · External reference
Cofactors and pathogens: Flavin mononucleotide and flavin adenine dinucleotide (FAD) biosynthesis by the FAD synthase from Brucella ovis
10.1002/iub.2576 · 2022 · External reference
Structure and mechanism of a eukaryotic FMN Adenylyltransferase
10.1016/j.jmb.2009.04.022 · 2009 · External reference
Evolutionary divergence of chloroplast FAD synthetase proteins
10.1186/1471-2148-10-311 · 2010 · External reference
Unresolved reference
2018 · External reference
Molecular characterization of FMN1, the structural gene for the monofunctional flavokinase of Saccharomyces cerevisiae
10.1074/jbc.m004621200 · 2000 · External reference
Crystal structure of Schizosaccharomyces pombe Riboflavin kinase reveals a novel ATP and riboflavin-binding fold
10.1016/s0022-2836(03)00059-7 · 2003 · External reference
Crystal structure of human riboflavin kinase reveals a β barrel fold and a novel active site arch
10.1016/s0969-2126(03)00024-8 · 2003 · External reference
Human riboflavin kinase: species-specific traits in the biosynthesis of the FMN cofactor
10.1096/fj.202000566r · 2020 · External reference
Structural analysis of FAD synthetase from Corynebacterium ammoniagenes
10.1186/1471-2180-8-160 · 2008 · External reference
Truncated FAD synthetase for direct biocatalytic conversion of riboflavin and analogs to their corresponding flavin mononucleotides
10.1093/protein/gzt055 · 2013 · External reference
Structural insights into the synthesis of FMN in prokaryotic organisms
10.1107/s1399004715019641 · 2015 · External reference
Molecular insights into the mechanism of substrate binding and catalysis of bifunctional FAD synthetase from Staphylococcus aureus
10.1016/j.biochi.2021.01.013 · 2021 · External reference
Oligomeric state in the crystal structure of modular FAD synthetase provides insights into its sequential catalysis in prokaryotes
10.1016/j.jmb.2010.05.018 · 2010 · External reference
The ribR gene encodes a monofunctional riboflavin kinase which is involved in regulation of the Bacillus subtilis riboflavin operon
10.1099/13500872-145-1-67 · 1999 · External reference
IVA cloning: a single-tube universal cloning system exploiting bacterial in vivo assembly
10.1038/srep27459 · 2016 · External reference
Microscale thermophoresis quantifies biomolecular interactions under previously challenging conditions
10.1016/j.ymeth.2012.12.005 · 2013 · External reference
AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
10.1002/jcc.21334 · 2010 · External reference
UCSF Chimera—A visualization system for exploratory research and analysis
10.1002/jcc.20084 · 2004 · External reference
Development of polyphosphate parameters for use with the AMBER force field
10.1002/jcc.10262 · 2003 · External reference
Unresolved reference
2016 · External reference
ff14SB: improving the accuracy of protein side chain and backbone parameters from ff99SB
10.1021/acs.jctc.5b00255 · 2015 · External reference
Antechamber: an accessory software package for molecular mechanical calculations
2001 · External reference
Unresolved reference
2014 · External reference
PTRAJ and CPPTRAJ: software for processing and analysis of molecular dynamics trajectory data
10.1021/ct400341p · 2013 · External reference
Unresolved reference
2015 · External reference
The generation of new protein functions by the combination of domains
10.1016/j.str.2006.11.009 · 2007 · External reference
Heterodimeric structure of superoxide dismutase in complex with its metallochaperone
10.1038/nsb0901-751 · 2001 · External reference
The antibiotics roseoflavin and 8-demethyl-8-amino-riboflavin from Streptomyces davawensis are metabolized by human flavokinase and human FAD synthetase
10.1016/j.bcp.2011.08.029 · 2011 · External reference
Role of linkers in communication between protein modules
10.1016/s1367-5931(99)00046-0 · 2000 · External reference
Structures and mechanism of transcription initiation by bacterial ECF factors
10.1093/nar/gkz470 · 2019 · External reference
