메뉴 건너뛰기




Volumn 1844, Issue 12, 2014, Pages 2086-2095

Significance of redox-active cysteines in human FAD synthase isoform 2

Author keywords

Disulfide bridge; FMN adenylyltransferase; Human FAD synthase; Mercury toxicity; Redox sensing; Thiol

Indexed keywords

ADENOSINE 3' PHOSPHATE 5' PHOSPHOSULFATE; CYSTEINE DERIVATIVE; FLAVINE ADENINE NUCLEOTIDE; MOLYBDOPTERIN; OXIDOREDUCTASE; SYNTHETASE; THIOL REAGENT;

EID: 84907646942     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2014.08.005     Document Type: Article
Times cited : (16)

References (30)
  • 1
    • 0024601564 scopus 로고
    • Mechanisms of flavoprotein-catalyzed reactions
    • S. Ghisla, and V. Massey Mechanisms of flavoprotein-catalyzed reactions Eur. J. Biochem. 181 1989 1 17
    • (1989) Eur. J. Biochem. , vol.181 , pp. 1-17
    • Ghisla, S.1    Massey, V.2
  • 2
    • 0033851115 scopus 로고    scopus 로고
    • The chemical and biological versatility of riboflavin
    • V. Massey The chemical and biological versatility of riboflavin Biochem. Soc. Trans. 28 2000 283 296
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 283-296
    • Massey, V.1
  • 4
    • 0028950476 scopus 로고
    • Cloning and characterization of FAD1, the structural gene for flavin adenine dinucleotide synthetase of Saccharomyces cerevisiae
    • M. Wu, B. Repetto, D.M. Glerum, and A. Tzagoloff Cloning and characterization of FAD1, the structural gene for flavin adenine dinucleotide synthetase of Saccharomyces cerevisiae Mol. Cell. Biol. 15 1995 264 271
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 264-271
    • Wu, M.1    Repetto, B.2    Glerum, D.M.3    Tzagoloff, A.4
  • 5
    • 0032493472 scopus 로고    scopus 로고
    • Proposed steady-state kinetic mechanism for Corynebacterium ammoniagenes FAD synthetase produced by Escherichia coli
    • I. Efimov, V. Kuusk, X. Zhang, and W.S. McIntire Proposed steady-state kinetic mechanism for Corynebacterium ammoniagenes FAD synthetase produced by Escherichia coli Biochemistry 37 1998 9716 9723
    • (1998) Biochemistry , vol.37 , pp. 9716-9723
    • Efimov, I.1    Kuusk, V.2    Zhang, X.3    McIntire, W.S.4
  • 6
    • 0018716780 scopus 로고
    • Flavokinase and FAD synthetase from Bacillus subtilis specific for reduced flavins
    • E.B. Kearney, J. Goldenberg, J. Lipsick, and M. Perl Flavokinase and FAD synthetase from Bacillus subtilis specific for reduced flavins J. Biol. Chem. 254 1979 9551 9557
    • (1979) J. Biol. Chem. , vol.254 , pp. 9551-9557
    • Kearney, E.B.1    Goldenberg, J.2    Lipsick, J.3    Perl, M.4
  • 8
    • 65549115599 scopus 로고    scopus 로고
    • Structure and mechanism of a eukaryotic FMN adenylyltransferase
    • C. Huerta, D. Borek, M. Machius, N.V. Grishin, and H. Zhang Structure and mechanism of a eukaryotic FMN adenylyltransferase J. Mol. Biol. 389 2009 388 400
    • (2009) J. Mol. Biol. , vol.389 , pp. 388-400
    • Huerta, C.1    Borek, D.2    MacHius, M.3    Grishin, N.V.4    Zhang, H.5
  • 13
    • 84871700620 scopus 로고    scopus 로고
    • Bacterial over-expression and purification of the 3′phosphoadenosine 5′phosphosulfate (PAPS) reductase domain of human FAD synthase: Functional characterization and homology modeling
    • A. Miccolis, M. Galluccio, T.A. Giancaspero, C. Indiveri, and M. Barile Bacterial over-expression and purification of the 3′phosphoadenosine 5′phosphosulfate (PAPS) reductase domain of human FAD synthase: functional characterization and homology modeling Int. J. Mol. Sci. 13 2012 16880 16898
    • (2012) Int. J. Mol. Sci. , vol.13 , pp. 16880-16898
    • Miccolis, A.1    Galluccio, M.2    Giancaspero, T.A.3    Indiveri, C.4    Barile, M.5
  • 14
    • 79952752769 scopus 로고    scopus 로고
    • The history of the discovery of the molybdenum cofactor and novel aspects of its biosynthesis in bacteria
    • S. Leimkuhler, M.M. Wuebbens, and K.V. Rajagopalan The history of the discovery of the molybdenum cofactor and novel aspects of its biosynthesis in bacteria Coord. Chem. Rev. 255 2011 1129 1144
    • (2011) Coord. Chem. Rev. , vol.255 , pp. 1129-1144
    • Leimkuhler, S.1    Wuebbens, M.M.2    Rajagopalan, K.V.3
  • 15
    • 68949107281 scopus 로고    scopus 로고
    • Molybdenum cofactors, enzymes and pathways
    • G. Schwarz, R.R. Mendel, and M.W. Ribbe Molybdenum cofactors, enzymes and pathways Nature 460 2009 839 847
    • (2009) Nature , vol.460 , pp. 839-847
    • Schwarz, G.1    Mendel, R.R.2    Ribbe, M.W.3
  • 18
    • 0023664455 scopus 로고
    • Complete purification and general characterization of FAD synthetase from rat liver
    • M. Oka, and D.B. McCormick Complete purification and general characterization of FAD synthetase from rat liver J. Biol. Chem. 262 1987 7418 7422
    • (1987) J. Biol. Chem. , vol.262 , pp. 7418-7422
    • Oka, M.1    McCormick, D.B.2
  • 19
    • 80555149405 scopus 로고    scopus 로고
    • The antibiotics roseoflavin and 8-demethyl-8-amino-riboflavin from Streptomyces davawensis are metabolized by human flavokinase and human FAD synthetase
    • D.B. Pedrolli, S. Nakanishi, M. Barile, M. Mansurova, E.C. Carmona, A. Lux, W. Gartner, and M. Mack The antibiotics roseoflavin and 8-demethyl-8-amino-riboflavin from Streptomyces davawensis are metabolized by human flavokinase and human FAD synthetase Biochem. Pharmacol. 82 2011 1853 1859
    • (2011) Biochem. Pharmacol. , vol.82 , pp. 1853-1859
    • Pedrolli, D.B.1    Nakanishi, S.2    Barile, M.3    Mansurova, M.4    Carmona, E.C.5    Lux, A.6    Gartner, W.7    MacK, M.8
  • 21
    • 0037047032 scopus 로고    scopus 로고
    • Site-directed mutagenesis and chemical modification of the six native cysteine residues of the rat mitochondrial carnitine carrier: Implications for the role of cysteine-136
    • C. Indiveri, N. Giangregorio, V. Iacobazzi, and F. Palmieri Site-directed mutagenesis and chemical modification of the six native cysteine residues of the rat mitochondrial carnitine carrier: implications for the role of cysteine-136 Biochemistry 41 2002 8649 8656
    • (2002) Biochemistry , vol.41 , pp. 8649-8656
    • Indiveri, C.1    Giangregorio, N.2    Iacobazzi, V.3    Palmieri, F.4
  • 22
    • 21244484274 scopus 로고    scopus 로고
    • Identification by site-directed mutagenesis and chemical modification of three vicinal cysteine residues in rat mitochondrial carnitine/acylcarnitine transporter
    • A. Tonazzi, N. Giangregorio, C. Indiveri, and F. Palmieri Identification by site-directed mutagenesis and chemical modification of three vicinal cysteine residues in rat mitochondrial carnitine/acylcarnitine transporter J. Biol. Chem. 280 2005 19607 19612
    • (2005) J. Biol. Chem. , vol.280 , pp. 19607-19612
    • Tonazzi, A.1    Giangregorio, N.2    Indiveri, C.3    Palmieri, F.4
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 24
    • 0030721976 scopus 로고    scopus 로고
    • Flavin adenine dinucleotide and flavin mononucleotide metabolism in rat liver - The occurrence of FAD pyrophosphatase and FMN phosphohydrolase in isolated mitochondria
    • M. Barile, C. Brizio, C. De Virgilio, S. Delfine, E. Quagliariello, and S. Passarella Flavin adenine dinucleotide and flavin mononucleotide metabolism in rat liver - the occurrence of FAD pyrophosphatase and FMN phosphohydrolase in isolated mitochondria Eur. J. Biochem. 249 1997 777 785
    • (1997) Eur. J. Biochem. , vol.249 , pp. 777-785
    • Barile, M.1    Brizio, C.2    De Virgilio, C.3    Delfine, S.4    Quagliariello, E.5    Passarella, S.6
  • 25
    • 0032401864 scopus 로고    scopus 로고
    • Evaluation of methods for the quantitation of cysteines in proteins
    • S.K. Wright, and R.E. Viola Evaluation of methods for the quantitation of cysteines in proteins Anal. Biochem. 265 1998 8 14
    • (1998) Anal. Biochem. , vol.265 , pp. 8-14
    • Wright, S.K.1    Viola, R.E.2
  • 26
    • 0015968884 scopus 로고
    • Reactions of thiosulfate and sulfite ions with DTNB: Interference in sulfhydryl group analysis
    • M. Man, and R.G. Bryant Reactions of thiosulfate and sulfite ions with DTNB: interference in sulfhydryl group analysis Anal. Biochem. 57 1974 429 431
    • (1974) Anal. Biochem. , vol.57 , pp. 429-431
    • Man, M.1    Bryant, R.G.2
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 4444224306 scopus 로고    scopus 로고
    • Over-expression in Escherichia coli, functional characterization and refolding of rat dimethylglycine dehydrogenase
    • C. Brizio, R. Brandsch, D. Bufano, L. Pochini, C. Indiveri, and M. Barile Over-expression in Escherichia coli, functional characterization and refolding of rat dimethylglycine dehydrogenase Protein Expr. Purif. 37 2004 434 442
    • (2004) Protein Expr. Purif. , vol.37 , pp. 434-442
    • Brizio, C.1    Brandsch, R.2    Bufano, D.3    Pochini, L.4    Indiveri, C.5    Barile, M.6
  • 29
    • 84857315113 scopus 로고    scopus 로고
    • Silencing of FAD synthase gene in Caenorhabditis elegans upsets protein homeostasis and impacts on complex behavioral patterns
    • V.C. Liuzzi, T.A. Giancaspero, E. Gianazza, C. Banfi, M. Barile, and C. De Giorgi Silencing of FAD synthase gene in Caenorhabditis elegans upsets protein homeostasis and impacts on complex behavioral patterns Biochim. Biophys. Acta 1820 2012 521 531
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 521-531
    • Liuzzi, V.C.1    Giancaspero, T.A.2    Gianazza, E.3    Banfi, C.4    Barile, M.5    De Giorgi, C.6
  • 30
    • 71549143840 scopus 로고    scopus 로고
    • Disulfides as redox switches: From molecular mechanisms to functional significance
    • M.A. Wouters, S.W. Fan, and N.L. Haworth Disulfides as redox switches: from molecular mechanisms to functional significance Antioxid. Redox Signal. 12 2010 53 91
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 53-91
    • Wouters, M.A.1    Fan, S.W.2    Haworth, N.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.