메뉴 건너뛰기




Volumn 8, Issue , 2008, Pages

Structural analysis of FAD synthetase from Corynebacterium ammoniagenes

Author keywords

[No Author keywords available]

Indexed keywords

FLAVINE ADENINE NUCLEOTIDE; FLAVINE ADENINE NUCLEOTIDE SYNTHETASE; NUCLEOTYDYLTRANSFERASE; RIBOFLAVIN KINASE; UNCLASSIFIED DRUG; FLAVINE MONONUCLEOTIDE; FMN ADENYLYLTRANSFERASE; NUCLEOTIDYLTRANSFERASE; RIBOFLAVIN DERIVATIVE;

EID: 54949103490     PISSN: 14712180     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/1471-2180-8-160     Document Type: Article
Times cited : (49)

References (37)
  • 3
    • 0023664455 scopus 로고
    • Complete purification and general characterization of FAD synthetase from rat liver
    • 3034893
    • Complete purification and general characterization of FAD synthetase from rat liver. M Oka DB McCormick, J Biol Chem 1987 262 15 7418 7422 3034893
    • (1987) J Biol Chem , vol.262 , Issue.15 , pp. 7418-7422
    • Oka, M.1    McCormick, D.B.2
  • 4
    • 0019332310 scopus 로고
    • Affinity chromatographic purification and properties of flavokinase (ATP:riboflavin 5'-phosphotransferase) from rat liver
    • 6243635
    • Affinity chromatographic purification and properties of flavokinase (ATP:riboflavin 5'-phosphotransferase) from rat liver. AH Merrill Jr DB McCormick, J Biol Chem 1980 255 4 1335 1338 6243635
    • (1980) J Biol Chem , vol.255 , Issue.4 , pp. 1335-1338
    • Merrill Jr., A.H.1    McCormick, D.B.2
  • 6
    • 33845928198 scopus 로고    scopus 로고
    • Over-expression in Escherichia coli, purification and characterization of isoform 2 of human FAD synthetase
    • 17049878
    • Over-expression in Escherichia coli, purification and characterization of isoform 2 of human FAD synthetase. M Galluccio C Brizio EM Torchetti P Ferranti E Gianazza C Indiveri M Barile, Protein Expr Purif 2007 52 1 175 181 17049878
    • (2007) Protein Expr Purif , vol.52 , Issue.1 , pp. 175-181
    • Galluccio, M.1    Brizio, C.2    Torchetti, E.M.3    Ferranti, P.4    Gianazza, E.5    Indiveri, C.6    Barile, M.7
  • 7
    • 0022970597 scopus 로고
    • Purification and characterization of FAD synthetase from Brevibacterium ammoniagenes
    • 3023344
    • Purification and characterization of FAD synthetase from Brevibacterium ammoniagenes. DJ Manstein EF Pai, J Biol Chem 1986 261 34 16169 16173 3023344
    • (1986) J Biol Chem , vol.261 , Issue.34 , pp. 16169-16173
    • Manstein, D.J.1    Pai, E.F.2
  • 8
    • 39749093132 scopus 로고    scopus 로고
    • The bifunctional flavokinase/flavin adenine dinucleotide synthetase from Streptomyces davawensis produces inactive flavin cofactors and is not involved in resistance to the antibiotic roseoflavin
    • 18156273
    • The bifunctional flavokinase/flavin adenine dinucleotide synthetase from Streptomyces davawensis produces inactive flavin cofactors and is not involved in resistance to the antibiotic roseoflavin. S Grill S Busenbender M Pfeiffer U Kohler M Mack, J Bacteriol 2008 190 5 1546 1553 18156273
    • (2008) J Bacteriol , vol.190 , Issue.5 , pp. 1546-1553
    • Grill, S.1    Busenbender, S.2    Pfeiffer, M.3    Kohler, U.4    MacK, M.5
  • 9
    • 0032493472 scopus 로고    scopus 로고
    • Proposed steady-state kinetic mechanism for Corynebacterium ammoniagenes FAD synthetase produced by Escherichia coli
    • 9657684
    • Proposed steady-state kinetic mechanism for Corynebacterium ammoniagenes FAD synthetase produced by Escherichia coli. I Efimov V Kuusk X Zhang WS McIntire, Biochemistry 1998 37 27 9716 9723 9657684
    • (1998) Biochemistry , vol.37 , Issue.27 , pp. 9716-9723
    • Efimov, I.1    Kuusk, V.2    Zhang, X.3    McIntire, W.S.4
  • 10
    • 0031420511 scopus 로고    scopus 로고
    • Syntheses and applications of flavin analogs as active site probes for flavoproteins
    • 9211339
    • Syntheses and applications of flavin analogs as active site probes for flavoproteins. YV Murthy V Massey, Methods Enzymol 1997 280 436 460 9211339
    • (1997) Methods Enzymol , vol.280 , pp. 436-460
    • Murthy, Y.V.1    Massey, V.2
  • 11
    • 0028798483 scopus 로고
    • Cloning of FAD synthetase gene from Corynebacterium ammoniagenes and its application to FAD and FMN production
    • 7765913
    • Cloning of FAD synthetase gene from Corynebacterium ammoniagenes and its application to FAD and FMN production. T Hagihara T Fujio K Aisaka, Appl Microbiol Biotechnol 1995 42 5 724 729 7765913
    • (1995) Appl Microbiol Biotechnol , vol.42 , Issue.5 , pp. 724-729
    • Hagihara, T.1    Fujio, T.2    Aisaka, K.3
  • 12
    • 85007873382 scopus 로고
    • Nucleotide sequence of the FAD synthetase gene from Corynebacterium ammoniagenes and its expression in Escherichia coli
    • 7772835
    • Nucleotide sequence of the FAD synthetase gene from Corynebacterium ammoniagenes and its expression in Escherichia coli. S Nakagawa A Igarashi T Ohta T Hagihara T Fujio K Aisaka, Biosci Biotechnol Biochem 1995 59 4 694 702 7772835
    • (1995) Biosci Biotechnol Biochem , vol.59 , Issue.4 , pp. 694-702
    • Nakagawa, S.1    Igarashi, A.2    Ohta, T.3    Hagihara, T.4    Fujio, T.5    Aisaka, K.6
  • 13
    • 0037219142 scopus 로고    scopus 로고
    • A conserved domain in prokaryotic bifunctional FAD synthetases can potentially catalyze nucleotide transfer
    • 12517446
    • A conserved domain in prokaryotic bifunctional FAD synthetases can potentially catalyze nucleotide transfer. A Krupa K Sandhya N Srinivasan S Jonnalagadda, Trends Biochem Sci 2003 28 1 9 12 12517446
    • (2003) Trends Biochem Sci , vol.28 , Issue.1 , pp. 9-12
    • Krupa, A.1    Sandhya, K.2    Srinivasan, N.3    Jonnalagadda, S.4
  • 14
    • 0041919534 scopus 로고    scopus 로고
    • Crystal structure of a flavin-binding protein from Thermotoga maritima
    • 12910462
    • Crystal structure of a flavin-binding protein from Thermotoga maritima. W Wang R Kim J Jancarik H Yokota SH Kim, Proteins 2003 52 4 633 635 12910462
    • (2003) Proteins , vol.52 , Issue.4 , pp. 633-635
    • Wang, W.1    Kim, R.2    Jancarik, J.3    Yokota, H.4    Kim, S.H.5
  • 15
    • 10844293516 scopus 로고    scopus 로고
    • Crystal structure of flavin binding to FAD synthetase of Thermotoga maritima
    • 15468322
    • Crystal structure of flavin binding to FAD synthetase of Thermotoga maritima. W Wang R Kim H Yokota SH Kim, Proteins 2005 58 1 246 248 15468322
    • (2005) Proteins , vol.58 , Issue.1 , pp. 246-248
    • Wang, W.1    Kim, R.2    Yokota, H.3    Kim, S.H.4
  • 17
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • 7984417
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. JD Thompson DG Higgins TJ Gibson, Nucleic Acids Res 1994 22 22 4673 4680 7984417
    • (1994) Nucleic Acids Res , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 19
    • 0036172167 scopus 로고    scopus 로고
    • Geno3D: Automatic comparative molecular modelling of protein
    • 11836238
    • Geno3D: automatic comparative molecular modelling of protein. C Combet M Jambon G Deleage C Geourjon, Bioinformatics 2002 18 1 213 214 11836238
    • (2002) Bioinformatics , vol.18 , Issue.1 , pp. 213-214
    • Combet, C.1    Jambon, M.2    Deleage, G.3    Geourjon, C.4
  • 20
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • PROCHECK: a program to check the stereochemical quality of protein structures. RA Laskowski MW MacArthur DS Moss JM Thornton, J Appl Cryst 1993 26 283 291
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 21
    • 0037336031 scopus 로고    scopus 로고
    • Crystal structure of human riboflavin kinase reveals a beta barrel fold and a novel active site arch
    • 12623014
    • Crystal structure of human riboflavin kinase reveals a beta barrel fold and a novel active site arch. S Karthikeyan Q Zhou F Mseeh NV Grishin AL Osterman H Zhang, Structure 2003 11 3 265 273 12623014
    • (2003) Structure , vol.11 , Issue.3 , pp. 265-273
    • Karthikeyan, S.1    Zhou, Q.2    Mseeh, F.3    Grishin, N.V.4    Osterman, A.L.5    Zhang, H.6
  • 22
    • 0242381351 scopus 로고    scopus 로고
    • Ligand binding-induced conformational changes in riboflavin kinase: Structural basis for the ordered mechanism
    • 14580199
    • Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism. S Karthikeyan Q Zhou AL Osterman H Zhang, Biochemistry 2003 42 43 12532 12538 14580199
    • (2003) Biochemistry , vol.42 , Issue.43 , pp. 12532-12538
    • Karthikeyan, S.1    Zhou, Q.2    Osterman, A.L.3    Zhang, H.4
  • 23
    • 0037424602 scopus 로고    scopus 로고
    • Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold
    • 12595258
    • Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold. S Bauer K Kemter A Bacher R Huber M Fischer S Steinbacher, J Mol Biol 2003 326 5 1463 1473 12595258
    • (2003) J Mol Biol , vol.326 , Issue.5 , pp. 1463-1473
    • Bauer, S.1    Kemter, K.2    Bacher, A.3    Huber, R.4    Fischer, M.5    Steinbacher, S.6
  • 24
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • 2025413
    • Improved methods for building protein models in electron density maps and the location of errors in these models. TA Jones JY Zou SW Cowan M Kjeldgaard, Acta Crystallogr A 1991 47 Pt 2 110 119 2025413
    • (1991) Acta Crystallogr a , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 25
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • 9504803
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. N Guex MC Peitsch, Electrophoresis 1997 18 15 2714 2723 9504803
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 27
    • 0029320145 scopus 로고
    • A versatile quick-prep of genomic DNA from Gram-positive bacteria
    • 7638902
    • A versatile quick-prep of genomic DNA from Gram-positive bacteria. A Pospiech B Neumann, Trends in Genetics 1995 11 6 217 218 7638902
    • (1995) Trends in Genetics , vol.11 , Issue.6 , pp. 217-218
    • Pospiech, A.1    Neumann, B.2
  • 29
    • 0037194931 scopus 로고    scopus 로고
    • Dynamic conformations of flavin adenine dinucleotide: Simulated molecular dynamics of the flavin cofactor related to the time-resolved fluorescence characteristics
    • Dynamic conformations of flavin adenine dinucleotide: Simulated molecular dynamics of the flavin cofactor related to the time-resolved fluorescence characteristics. PAW van den Berg KA Feenstra AE Mark HJC Berendsen AJWG Visser, J Phys Chem B 2002 106 34 8858 8869
    • (2002) J Phys Chem B , vol.106 , Issue.34 , pp. 8858-8869
    • Den Van, W.A.B.P.1    Feenstra, K.A.2    Mark, A.E.3    Berendsen, H.J.C.4    Visser, A.J.W.G.5
  • 30
    • 0000235244 scopus 로고    scopus 로고
    • A prototypical cytidylyltransferase: CTP:glycerol-3-phosphate cytidylyltransferase from Bacillus subtilis
    • 10508782
    • A prototypical cytidylyltransferase: CTP:glycerol-3-phosphate cytidylyltransferase from Bacillus subtilis. CH Weber YS Park S Sanker C Kent ML Ludwig, Structure 1999 7 9 1113 1124 10508782
    • (1999) Structure , vol.7 , Issue.9 , pp. 1113-1124
    • Weber, C.H.1    Park, Y.S.2    Sanker, S.3    Kent, C.4    Ludwig, M.L.5
  • 33
    • 0035831542 scopus 로고    scopus 로고
    • + synthesis: Structures of Methanobacterium thermoautotrophicum NMN adenylyltransferase complexes
    • 11063748
    • + synthesis: structures of Methanobacterium thermoautotrophicum NMN adenylyltransferase complexes. V Saridakis D Christendat MS Kimber A Dharamsi AM Edwards EF Pai, J Biol Chem 2001 276 10 7225 7232 11063748
    • (2001) J Biol Chem , vol.276 , Issue.10 , pp. 7225-7232
    • Saridakis, V.1    Christendat, D.2    Kimber, M.S.3    Dharamsi, A.4    Edwards, A.M.5    Pai, E.F.6
  • 34
    • 0033561042 scopus 로고    scopus 로고
    • The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivity
    • 10205156
    • The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivity. T Izard A Geerlof, Embo J 1999 18 8 2021 2030 10205156
    • (1999) Embo J , vol.18 , Issue.8 , pp. 2021-2030
    • Izard, T.1    Geerlof, A.2
  • 37
    • 0036301087 scopus 로고    scopus 로고
    • The crystal structures of phosphopantetheine adenylyltransferase with bound substrates reveal the enzyme's catalytic mechanism
    • 11812124
    • The crystal structures of phosphopantetheine adenylyltransferase with bound substrates reveal the enzyme's catalytic mechanism. T Izard, J Mol Biol 2002 315 4 487 495 11812124
    • (2002) J Mol Biol , vol.315 , Issue.4 , pp. 487-495
    • Izard, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.