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Reference on EC 2.7.1.26 - riboflavin kinase

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Walsh, C.; Fisher, J.; Spencer, R.; Graham, D.W.; Ashton, W.T.; Brown, J.E.; Brown, R.D.; Rogers, E.F.
Chemical and enzymatic properties of riboflavin analogues
Biochemistry
17
1942-1951
1978
Corynebacterium ammoniagenes
Manually annotated by BRENDA team
Kearney, E.B.
The interaction of yeast flavokinase with riboflavin analogues
J. Biol. Chem.
194
747-754
1952
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Chassy, B.M.; Arsenis, C.; McCormick, D.B.
The effect of the length of the side chain of flavins on reactivity with flavokinase
J. Biol. Chem.
240
1338-1340
1965
Rattus norvegicus
Manually annotated by BRENDA team
McCormick, D.B.; Butler, R.C.
Substrate specificity of liver flavokinase
Biochim. Biophys. Acta
65
326-332
1962
Rattus norvegicus
-
Manually annotated by BRENDA team
Yamada, Y.; Merrill, A.; McCormick, D.N.
Probable reaction mechanisms of flavokinase and FAD synthetase from rat liver
Arch. Biochem. Biophys.
278
125-130
1990
Rattus norvegicus
Manually annotated by BRENDA team
Kasai, S.; Nakano, H.; Maeda, K.; Matsui, K.
Purification, properties, and function of flavokinase from rat intestinal mucosa
J. Biochem.
107
298-303
1990
Rattus norvegicus
Manually annotated by BRENDA team
Merrill, A.H.; McCormick, D.B.
Affinity chromatographic purification and properties of flavokinase (ATP:riboflavin 5-phosphotransferase) from rat liver
J. Biol. Chem.
255
1335-1338
1980
Rattus norvegicus
Manually annotated by BRENDA team
Mayhew, S.G.; Wassink, J.H.
Continuous fluorescence assay, partial purification and properties of flavokinase from Megasphaera elsdenii
Methods Enzymol.
66
323-327
1980
Megasphaera elsdenii
Manually annotated by BRENDA team
Mayhew, S.G.; Wassink, J.H.
A continuous fluorometric assay for flavokinase. Properties of flavokinase from Peptostreptococcus elsdenii
Biochim. Biophys. Acta
482
341-347
1977
Megasphaera elsdenii
Manually annotated by BRENDA team
Merrill, A.H.; McCormick, D.B.
Preparation and properties of immobilized flavokinase
Biotechnol. Bioeng.
21
1629-1638
1979
Rattus norvegicus
Manually annotated by BRENDA team
Sobhanaditya, J.; Rao, N.A.
Plant flavokinase. Affinity-chromatographic procedure for the purification of the enzyme from mung-bean (Phaseolus aureus) seeds and conformational changes on its interaction with orthophosphate
Biochem. J.
197
227-232
1981
Vigna radiata var. radiata
Manually annotated by BRENDA team
Kearny, E.B.; Goldenberg, J.; Lipsick, J.; Perl, M.
Flavokinase and FAD synthetase from Bacillus subtilis specific for reduced flavins
J. Biol. Chem.
254
9551-9557
1979
Bacillus subtilis
Manually annotated by BRENDA team
Manstein, D.J.; Pai, E.F.
Purification and characterization of FAD synthetase from Brevibacterium ammoniagenes
J. Biol. Chem.
261
16169-16173
1986
Corynebacterium ammoniagenes
Manually annotated by BRENDA team
Rajeswari, S.R.; Jonnalagadda, V.S.; Jonnalagadda, S.
Purification and characterization of flavokinase from Neurospora crassa
Indian J. Biochem. Biophys.
36
137-142
1999
Neurospora crassa
Manually annotated by BRENDA team
Bandyopadhyay, D.; Chatterjee, A.K.; Datta, A.G.
Effect of cadmium, mercury and copper on partially purified hepatic flavokinase of rat
Mol. Cell. Biochem.
167
73-80
1997
Rattus norvegicus
Manually annotated by BRENDA team
Cho, K.W.
Bioluminescent assay of bovine liver riboflavin kinase using a bacterial luciferase coupled reaction
J. Microbiol.
38
74-79
2000
Bos taurus
-
Manually annotated by BRENDA team
Solovieva, I.M.; Tarasov, K.V.; Perumov, D.A.
Main physicochemical features of monofunctional flavokinase from Bacillus subtilis
Biochemistry
68
177-181
2003
Bacillus subtilis
Manually annotated by BRENDA team
Mack, M.; van Loon, A.P.; Hohmann, H.P.
Regulation of riboflavin biosynthesis in Bacillus subtilis is affected by the activity of the flavokinase/flavin adenine dinucleotide synthetase encoded by ribC
J. Bacteriol.
180
950-955
1998
Bacillus subtilis (P54575), Bacillus subtilis
Manually annotated by BRENDA team
Solovieva, I.M.; Kreneva, R.A.; Leak, D.J.; Perumov, D.A.
The ribR gene encodes a monofunctional riboflavin kinase which is involved in regulation of the Bacillus subtilis riboflavin operon
Microbiology
145
67-73
1999
Bacillus subtilis
Manually annotated by BRENDA team
Bandyopadhyay, D.; Chatterjee, A.K.; Datta, A.G.
Effect of cadmium on purified hepatic flavokinase: involvement of reactive -SH group(s) in the inactivation of flavokinase by cadmium
Life Sci.
60
1891-1903
1997
Rattus norvegicus
Manually annotated by BRENDA team
Bauer, S.; Kemter, K.; Bacher, A.; Huber, R.; Fischer, M.; Steinbacher, S.
Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold
J. Mol. Biol.
326
1463-1473
2003
Schizosaccharomyces pombe (O74866), Schizosaccharomyces pombe
Manually annotated by BRENDA team
Karthikeyan, S.; Zhou, Q.; Mseeh, F.; Grishin, N.V.; Osterman, A.L.; Zhang, H.
Crystal structure of human riboflavin kinase reveals a beta barrel fold and a novel active site arch
Structure
11
265-273
2003
Homo sapiens (Q969G6), Homo sapiens
Manually annotated by BRENDA team
Karthikeyan, S.; Zhou, Q.; Osterman, A.L.; Zhang, H.
Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism
Biochemistry
42
12532-12538
2003
Homo sapiens (Q969G6), Homo sapiens
Manually annotated by BRENDA team
Solovieva, I.M.; Kreneva, R.A.; Errais Lopes, L.; Perumov, D.A.
The riboflavin kinase encoding gene ribR of Bacillus subtilis is a part of a 10 kb operon, which is negatively regulated by the yrzC gene product
FEMS Microbiol. Lett.
243
51-58
2005
Bacillus subtilis
Manually annotated by BRENDA team
Higashitsuji, Y.; Angerer, A.; Berghaus, S.; Hobl, B.; Mack, M.
RibR, a possible regulator of the Bacillus subtilis riboflavin biosynthetic operon, in vivo interacts with the 5-untranslated leader of rib mRNA
FEMS Microbiol. Lett.
274
48-54
2007
Bacillus subtilis
Manually annotated by BRENDA team
Sandoval, F.J.; Roje, S.
An FMN hydrolase is fused to a riboflavin kinase homolog in plants
J. Biol. Chem.
280
38337-38345
2005
Arabidopsis thaliana
Manually annotated by BRENDA team
Grill, S.; Busenbender, S.; Pfeiffer, M.; Koehler, U.; Mack, M.
The bifunctional flavokinase/flavin adenine dinucleotide synthetase from Streptomyces davawensis produces inactive flavin cofactors and is not involved in resistance to the antibiotic roseoflavin
J. Bacteriol.
190
1546-1553
2008
Bacillus subtilis, Streptomyces davaonensis (A3FM23), Streptomyces davaonensis
Manually annotated by BRENDA team
Giancaspero, T.A.; Locato, V.; de Pinto, M.C.; De Gara, L.; Barile, M.
The occurrence of riboflavin kinase and FAD synthetase ensures FAD synthesis in tobacco mitochondria and maintenance of cellular redox status
FEBS J.
276
219-231
2009
Nicotiana tabacum
Manually annotated by BRENDA team
Yazdanpanah, B.; Wiegmann, K.; Tchikov, V.; Krut, O.; Pongratz, C.; Schramm, M.; Kleinridders, A.; Wunderlich, T.; Kashkar, H.; Utermoehlen, O.; Bruening, J.C.; Schuetze, S.; Kroenke, M.
Riboflavin kinase couples TNF receptor 1 to NADPH oxidase
Nature
460
1159-1163
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Serrano, A.; Frago, S.; Herguedas, B.; Martinez-Julvez, M.; Velazquez-Campoy, A.; Medina, M.
Key residues at the riboflavin kinase catalytic site of the bifunctional riboflavin kinase/FMN adenylyltransferase from Corynebacterium ammoniagenes
Cell Biochem. Biophys.
65
57-68
2013
Corynebacterium ammoniagenes
Manually annotated by BRENDA team
Serrano, A.; Frago, S.; Velazquez-Campoy, A.; Medina, M.
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
Int. J. Mol. Sci.
13
14492-14517
2012
Corynebacterium ammoniagenes (Q59263), Corynebacterium ammoniagenes
Manually annotated by BRENDA team
Park, K.J.; Lee, C.H.; Kim, A.; Jeong, K.J.; Kim, C.H.; Kim, Y.S.
Death receptors 4 and 5 activate Nox1 NADPH oxidase through riboflavin kinase to induce reactive oxygen species-mediated apoptotic cell death
J. Biol. Chem.
287
3313-3325
2012
Homo sapiens
Manually annotated by BRENDA team
Herguedas, B.; Lans, I.; Sebastian, M.; Hermoso, J.A.; Martinez-Julvez, M.; Medina, M.
Structural insights into the synthesis of FMN in prokaryotic organisms
Acta Crystallogr. Sect. D
71
2526-2542
2015
Corynebacterium ammoniagenes (Q59263), Corynebacterium ammoniagenes
Manually annotated by BRENDA team
Huerta, C.; Grishin, N.V.; Zhang, H.
The super mutant of yeast FMN adenylyltransferase enhances the enzyme turnover rate by attenuating product inhibition
Biochemistry
52
3615-3617
2013
[Candida] glabrata (Q6FNA9)
Manually annotated by BRENDA team
Serrano, A.; Sebastian, M.; Arilla-Luna, S.; Baquedano, S.; Pallares, M.C.; Lostao, A.; Herguedas, B.; Velazquez-Campoy, A.; Martinez-Julvez, M.; Medina, M.
Quaternary organization in a bifunctional prokaryotic FAD synthetase: Involvement of an arginine at its adenylyltransferase module on the riboflavin kinase activity
Biochim. Biophys. Acta
1854
897-906
2015
Corynebacterium ammoniagenes (Q59263), Corynebacterium ammoniagenes
Manually annotated by BRENDA team
Iamurri, S.M.; Daugherty, A.B.; Edmondson, D.E.; Lutz, S.
Truncated FAD synthetase for direct biocatalytic conversion of riboflavin and analogs to their corresponding flavin mononucleotides
Protein Eng. Des. Sel.
26
791-795
2013
Corynebacterium ammoniagenes (Q59263), Corynebacterium ammoniagenes
Manually annotated by BRENDA team
Anoz-Carbonell, E.; Rivero, M.; Polo, V.; Velazquez-Campoy, A.; Medina, M.
Human riboflavin kinase species-specific traits in the biosynthesis of the FMN cofactor
FASEB J.
34
10871-10886
2020
Homo sapiens (Q969G6), Homo sapiens
Manually annotated by BRENDA team
Sebastian, M.; Serrano, A.; Velazquez-Campoy, A.; Medina, M.
Kinetics and thermodynamics of the protein-ligand interactions in the riboflavin kinase activity of the FAD synthetase from Corynebacterium ammoniagenes
Sci. Rep.
7
7281
2017
Corynebacterium ammoniagenes (Q59263), Corynebacterium ammoniagenes
Manually annotated by BRENDA team