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Items: 1 to 20 of 162

2.

Key residues at the riboflavin kinase catalytic site of the bifunctional riboflavin kinase/FMN adenylyltransferase from Corynebacterium ammoniagenes.

Serrano A, Frago S, Herguedas B, Martínez-Júlvez M, Velázquez-Campoy A, Medina M.

Cell Biochem Biophys. 2013 Jan;65(1):57-68. doi: 10.1007/s12013-012-9403-9.

PMID:
22892871
3.

Structural insights into the synthesis of FMN in prokaryotic organisms.

Herguedas B, Lans I, Sebastián M, Hermoso JA, Martínez-Júlvez M, Medina M.

Acta Crystallogr D Biol Crystallogr. 2015 Dec 1;71(Pt 12):2526-42. doi: 10.1107/S1399004715019641. Epub 2015 Nov 27.

PMID:
26627660
4.

Oligomeric state in the crystal structure of modular FAD synthetase provides insights into its sequential catalysis in prokaryotes.

Herguedas B, Martínez-Júlvez M, Frago S, Medina M, Hermoso JA.

J Mol Biol. 2010 Jul 9;400(2):218-30. doi: 10.1016/j.jmb.2010.05.018. Epub 2010 May 13.

PMID:
20471397
5.

Kinetics and thermodynamics of the protein-ligand interactions in the riboflavin kinase activity of the FAD synthetase from Corynebacterium ammoniagenes.

Sebastián M, Serrano A, Velázquez-Campoy A, Medina M.

Sci Rep. 2017 Aug 4;7(1):7281. doi: 10.1038/s41598-017-07875-5.

6.

Structural analysis of FAD synthetase from Corynebacterium ammoniagenes.

Frago S, Martínez-Júlvez M, Serrano A, Medina M.

BMC Microbiol. 2008 Sep 23;8:160. doi: 10.1186/1471-2180-8-160.

7.

Quaternary organization in a bifunctional prokaryotic FAD synthetase: Involvement of an arginine at its adenylyltransferase module on the riboflavin kinase activity.

Serrano A, Sebastián M, Arilla-Luna S, Baquedano S, Pallarés MC, Lostao A, Herguedas B, Velázquez-Campoy A, Martínez-Júlvez M, Medina M.

Biochim Biophys Acta. 2015 Aug;1854(8):897-906. doi: 10.1016/j.bbapap.2015.03.005. Epub 2015 Mar 21.

PMID:
25801930
8.

Proposed steady-state kinetic mechanism for Corynebacterium ammoniagenes FAD synthetase produced by Escherichia coli.

Efimov I, Kuusk V, Zhang X, McIntire WS.

Biochemistry. 1998 Jul 7;37(27):9716-23.

PMID:
9657684
9.

Truncated FAD synthetase for direct biocatalytic conversion of riboflavin and analogs to their corresponding flavin mononucleotides.

Iamurri SM, Daugherty AB, Edmondson DE, Lutz S.

Protein Eng Des Sel. 2013 Dec;26(12):791-5. doi: 10.1093/protein/gzt055. Epub 2013 Oct 29.

PMID:
24170887
10.

The puzzle of ligand binding to Corynebacterium ammoniagenes FAD synthetase.

Frago S, Velázquez-Campoy A, Medina M.

J Biol Chem. 2009 Mar 13;284(11):6610-9. doi: 10.1074/jbc.M808142200. Epub 2009 Jan 11.

11.

Cloning of FAD synthetase gene from Corynebacterium ammoniagenes and its application to FAD and FMN production.

Hagihara T, Fujio T, Aisaka K.

Appl Microbiol Biotechnol. 1995 Jan;42(5):724-9.

PMID:
7765913
12.

The trimer interface in the quaternary structure of the bifunctional prokaryotic FAD synthetase from Corynebacterium ammoniagenes.

Serrano A, Sebastián M, Arilla-Luna S, Baquedano S, Herguedas B, Velázquez-Campoy A, Martínez-Júlvez M, Medina M.

Sci Rep. 2017 Mar 24;7(1):404. doi: 10.1038/s41598-017-00402-6.

13.

Archaeal RibL: a new FAD synthetase that is air sensitive.

Mashhadi Z, Xu H, Grochowski LL, White RH.

Biochemistry. 2010 Oct 12;49(40):8748-55. doi: 10.1021/bi100817q. Epub 2010 Sep 20.

PMID:
20822113
14.

Detection of a quaternary organization into dimer of trimers of Corynebacterium ammoniagenes FAD synthetase at the single-molecule level and at the in cell level.

Marcuello C, Arilla-Luna S, Medina M, Lostao A.

Biochim Biophys Acta. 2013 Mar;1834(3):665-76. doi: 10.1016/j.bbapap.2012.12.013. Epub 2013 Jan 3.

PMID:
23291469
15.

Synthesis and application of isotopically labeled flavin nucleotides.

Mishanina TV, Kohen A.

J Labelled Comp Radiopharm. 2015 Jul;58(9):370-5. doi: 10.1002/jlcr.3313. Epub 2015 Jul 7.

16.

Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold.

Bauer S, Kemter K, Bacher A, Huber R, Fischer M, Steinbacher S.

J Mol Biol. 2003 Mar 7;326(5):1463-73.

PMID:
12595258
18.

Saccharomyces cerevisiae mitochondria can synthesise FMN and FAD from externally added riboflavin and export them to the extramitochondrial phase.

Pallotta ML, Brizio C, Fratianni A, De Virgilio C, Barile M, Passarella S.

FEBS Lett. 1998 May 29;428(3):245-9.

19.

The prokaryotic FAD synthetase family: a potential drug target.

Serrano A, Ferreira P, Martínez-Júlvez M, Medina M.

Curr Pharm Des. 2013;19(14):2637-48. Review.

PMID:
23116401
20.

Probable reaction mechanisms of flavokinase and FAD synthetase from rat liver.

Yamada Y, Merrill AH Jr, McCormick DB.

Arch Biochem Biophys. 1990 Apr;278(1):125-30.

PMID:
2157358

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