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Volumn 7, Issue 1, 2012, Pages

Biochemical discrimination between selenium and sulfur 1: A single residue provides selenium specificity to human selenocysteine lyase

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; CYSTATHIONINE GAMMA LYASE; CYSTEINE; LYASE; SELENIDE; SELENIUM; SELENOCYSTEINE; SELENOCYSTEINE LYASE; SELENOPROTEIN; SULFUR; UNCLASSIFIED DRUG;

EID: 84861954783     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0030581     Document Type: Article
Times cited : (23)

References (44)
  • 1
    • 72649106932 scopus 로고    scopus 로고
    • The selenium to selenoprotein pathway in eukaryotes: more molecular partners than anticipated
    • Allmang C, Wurth L, Krol A, (2009) The selenium to selenoprotein pathway in eukaryotes: more molecular partners than anticipated. Biochim Biophys Acta 1790: 1415-1423.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 1415-1423
    • Allmang, C.1    Wurth, L.2    Krol, A.3
  • 2
    • 70349515119 scopus 로고    scopus 로고
    • The many levels of control on bacterial selenoprotein synthesis
    • Yoshizawa S, Bock A, (2009) The many levels of control on bacterial selenoprotein synthesis. Biochim Biophys Acta 1790: 1404-1414.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 1404-1414
    • Yoshizawa, S.1    Bock, A.2
  • 4
    • 33748753840 scopus 로고    scopus 로고
    • Selenium: from cancer prevention to DNA damage
    • Letavayova L, Vlckova V, Brozmanova J, (2006) Selenium: from cancer prevention to DNA damage. Toxicology 227: 1-14.
    • (2006) Toxicology , vol.227 , pp. 1-14
    • Letavayova, L.1    Vlckova, V.2    Brozmanova, J.3
  • 5
    • 4344604663 scopus 로고    scopus 로고
    • Selenium and selenoproteins in mammals: extraordinary, essential, enigmatic
    • Schomburg L, Schweizer U, Kohrle J, (2004) Selenium and selenoproteins in mammals: extraordinary, essential, enigmatic. Cell Mol Life Sci 61: 1988-1995.
    • (2004) Cell Mol Life Sci , vol.61 , pp. 1988-1995
    • Schomburg, L.1    Schweizer, U.2    Kohrle, J.3
  • 6
    • 33746189600 scopus 로고    scopus 로고
    • Practicalities of selenium supplementation in critically ill patients
    • Angstwurm MW, Gaertner R, (2006) Practicalities of selenium supplementation in critically ill patients. Curr Opin Clin Nutr Metab Care 9: 233-238.
    • (2006) Curr Opin Clin Nutr Metab Care , vol.9 , pp. 233-238
    • Angstwurm, M.W.1    Gaertner, R.2
  • 8
    • 33846343236 scopus 로고    scopus 로고
    • Biosynthesis of selenocysteine on its tRNA in eukaryotes
    • Xu XM, Carlson BA, Mix H, Zhang Y, Saira K, et al. (2007) Biosynthesis of selenocysteine on its tRNA in eukaryotes. PLoS Biol 5: e4.
    • (2007) PLoS Biol , vol.5
    • Xu, X.M.1    Carlson, B.A.2    Mix, H.3    Zhang, Y.4    Saira, K.5
  • 9
    • 33845763611 scopus 로고    scopus 로고
    • RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea
    • Yuan J, Palioura S, Salazar JC, Su D, O'Donoghue P, et al. (2006) RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea. Proc Natl Acad Sci U S A 103: 18923-18927.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 18923-18927
    • Yuan, J.1    Palioura, S.2    Salazar, J.C.3    Su, D.4    O'Donoghue, P.5
  • 10
    • 67650815502 scopus 로고    scopus 로고
    • The human SepSecS-tRNASec complex reveals the mechanism of selenocysteine formation
    • Palioura S, Sherrer RL, Steitz TA, Soll D, Simonovic M, (2009) The human SepSecS-tRNASec complex reveals the mechanism of selenocysteine formation. Science 325: 321-325.
    • (2009) Science , vol.325 , pp. 321-325
    • Palioura, S.1    Sherrer, R.L.2    Steitz, T.A.3    Soll, D.4    Simonovic, M.5
  • 11
    • 0026694318 scopus 로고
    • Selenite is a substrate for calf thymus thioredoxin reductase and thioredoxin and elicits a large non-stoichiometric oxidation of NADPH in the presence of oxygen
    • Kumar S, Bjornstedt M, Holmgren A, (1992) Selenite is a substrate for calf thymus thioredoxin reductase and thioredoxin and elicits a large non-stoichiometric oxidation of NADPH in the presence of oxygen. Eur J Biochem 207: 435-439.
    • (1992) Eur J Biochem , vol.207 , pp. 435-439
    • Kumar, S.1    Bjornstedt, M.2    Holmgren, A.3
  • 12
    • 0037155922 scopus 로고    scopus 로고
    • Methylseleninate is a substrate rather than an inhibitor of mammalian thioredoxin reductase. Implications for the antitumor effects of selenium
    • Gromer S, Gross JH, (2002) Methylseleninate is a substrate rather than an inhibitor of mammalian thioredoxin reductase. Implications for the antitumor effects of selenium. J Biol Chem 277: 9701-9706.
    • (2002) J Biol Chem , vol.277 , pp. 9701-9706
    • Gromer, S.1    Gross, J.H.2
  • 13
    • 0020490539 scopus 로고
    • Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme
    • Esaki N, Nakamura T, Tanaka H, Soda K, (1982) Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme. J Biol Chem 257: 4386-4391.
    • (1982) J Biol Chem , vol.257 , pp. 4386-4391
    • Esaki, N.1    Nakamura, T.2    Tanaka, H.3    Soda, K.4
  • 15
    • 34247623069 scopus 로고    scopus 로고
    • Selenocysteine beta-lyase and methylselenol demethylase in the metabolism of Se-methylated selenocompounds into selenide
    • Suzuki KT, Kurasaki K, Suzuki N, (2007) Selenocysteine beta-lyase and methylselenol demethylase in the metabolism of Se-methylated selenocompounds into selenide. Biochim Biophys Acta 1770: 1053-1061.
    • (2007) Biochim Biophys Acta , vol.1770 , pp. 1053-1061
    • Suzuki, K.T.1    Kurasaki, K.2    Suzuki, N.3
  • 16
    • 0034054495 scopus 로고    scopus 로고
    • cDNA cloning, purification, and characterization of mouse liver selenocysteine lyase. Candidate for selenium delivery protein in selenoprotein synthesis
    • Mihara H, Kurihara T, Watanabe T, Yoshimura T, Esaki N, (2000) cDNA cloning, purification, and characterization of mouse liver selenocysteine lyase. Candidate for selenium delivery protein in selenoprotein synthesis. J Biol Chem 275: 6195-6200.
    • (2000) J Biol Chem , vol.275 , pp. 6195-6200
    • Mihara, H.1    Kurihara, T.2    Watanabe, T.3    Yoshimura, T.4    Esaki, N.5
  • 17
    • 72649087329 scopus 로고    scopus 로고
    • Selenoprotein P-expression, functions, and roles in mammals
    • Burk RF, Hill KE, (2009) Selenoprotein P-expression, functions, and roles in mammals. Biochim Biophys Acta 1790: 1441-1447.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 1441-1447
    • Burk, R.F.1    Hill, K.E.2
  • 18
    • 0027049518 scopus 로고
    • Characterization of selenocysteine lyase in human tissues and its relationship to tissue selenium concentrations
    • Daher R, Van Lente F, (1992) Characterization of selenocysteine lyase in human tissues and its relationship to tissue selenium concentrations. J Trace Elem Electrolytes Health Dis 6: 189-194.
    • (1992) J Trace Elem Electrolytes Health Dis , vol.6 , pp. 189-194
    • Daher, R.1    van Lente, F.2
  • 19
    • 0032553428 scopus 로고    scopus 로고
    • The NIFS protein can function as a selenide delivery protein in the biosynthesis of selenophosphate
    • Lacourciere GM, Stadtman TC, (1998) The NIFS protein can function as a selenide delivery protein in the biosynthesis of selenophosphate. J Biol Chem 273: 30921-30926.
    • (1998) J Biol Chem , vol.273 , pp. 30921-30926
    • Lacourciere, G.M.1    Stadtman, T.C.2
  • 20
    • 0034093325 scopus 로고    scopus 로고
    • Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions
    • Mihara H, Kurihara T, Yoshimura T, Esaki N, (2000) Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions. J Biochem (Tokyo) 127: 559-567.
    • (2000) J Biochem (Tokyo) , vol.127 , pp. 559-567
    • Mihara, H.1    Kurihara, T.2    Yoshimura, T.3    Esaki, N.4
  • 21
    • 0036303444 scopus 로고    scopus 로고
    • Analysis of the E. coli NifS CsdB protein at 2.0 A reveals the structural basis for perselenide and persulfide intermediate formation
    • Lima CD, (2002) Analysis of the E. coli NifS CsdB protein at 2.0 A reveals the structural basis for perselenide and persulfide intermediate formation. J Mol Biol 315: 1199-1208.
    • (2002) J Mol Biol , vol.315 , pp. 1199-1208
    • Lima, C.D.1
  • 22
    • 0030963659 scopus 로고    scopus 로고
    • Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme
    • Mihara H, Kurihara T, Yoshimura T, Soda K, Esaki N, (1997) Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme. J Biol Chem 272: 22417-22424.
    • (1997) J Biol Chem , vol.272 , pp. 22417-22424
    • Mihara, H.1    Kurihara, T.2    Yoshimura, T.3    Soda, K.4    Esaki, N.5
  • 23
    • 33646349748 scopus 로고    scopus 로고
    • Trafficking in persulfides: delivering sulfur in biosynthetic pathways
    • Mueller EG, (2006) Trafficking in persulfides: delivering sulfur in biosynthetic pathways. Nat Chem Biol 2: 185-194.
    • (2006) Nat Chem Biol , vol.2 , pp. 185-194
    • Mueller, E.G.1
  • 24
    • 0242664733 scopus 로고    scopus 로고
    • The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli
    • Outten FW, Wood MJ, Munoz FM, Storz G, (2003) The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli. J Biol Chem 278: 45713-45719.
    • (2003) J Biol Chem , vol.278 , pp. 45713-45719
    • Outten, F.W.1    Wood, M.J.2    Munoz, F.M.3    Storz, G.4
  • 25
    • 77951749014 scopus 로고    scopus 로고
    • Structural basis for Fe-S cluster assembly and tRNA thiolation mediated by IscS protein-protein interactions
    • Shi R, Proteau A, Villarroya M, Moukadiri I, Zhang L, et al. (2010) Structural basis for Fe-S cluster assembly and tRNA thiolation mediated by IscS protein-protein interactions. PLoS Biol 8: e1000354.
    • (2010) PLoS Biol , vol.8
    • Shi, R.1    Proteau, A.2    Villarroya, M.3    Moukadiri, I.4    Zhang, L.5
  • 26
    • 0036204688 scopus 로고    scopus 로고
    • Selenium is mobilized in vivo from free selenocysteine and is incorporated specifically into formate dehydrogenase H and tRNA nucleosides
    • Lacourciere GM, (2002) Selenium is mobilized in vivo from free selenocysteine and is incorporated specifically into formate dehydrogenase H and tRNA nucleosides. J Bacteriol 184: 1940-1946.
    • (2002) J Bacteriol , vol.184 , pp. 1940-1946
    • Lacourciere, G.M.1
  • 27
    • 0034604544 scopus 로고    scopus 로고
    • Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate
    • Lacourciere GM, Mihara H, Kurihara T, Esaki N, Stadtman TC, (2000) Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate. J Biol Chem 275: 23769-23773.
    • (2000) J Biol Chem , vol.275 , pp. 23769-23773
    • Lacourciere, G.M.1    Mihara, H.2    Kurihara, T.3    Esaki, N.4    Stadtman, T.C.5
  • 28
    • 0033524427 scopus 로고    scopus 로고
    • Catalytic properties of selenophosphate synthetases: comparison of the selenocysteine-containing enzyme from Haemophilus influenzae with the corresponding cysteine-containing enzyme from Escherichia coli
    • Lacourciere GM, Stadtman TC, (1999) Catalytic properties of selenophosphate synthetases: comparison of the selenocysteine-containing enzyme from Haemophilus influenzae with the corresponding cysteine-containing enzyme from Escherichia coli. Proc Natl Acad Sci U S A 96: 44-48.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 44-48
    • Lacourciere, G.M.1    Stadtman, T.C.2
  • 29
    • 0037076318 scopus 로고    scopus 로고
    • The iscS gene is essential for the biosynthesis of 2-selenouridine in tRNA and the selenocysteine-containing formate dehydrogenase H
    • Mihara H, Kato S, Lacourciere GM, Stadtman TC, Kennedy RA, et al. (2002) The iscS gene is essential for the biosynthesis of 2-selenouridine in tRNA and the selenocysteine-containing formate dehydrogenase H. Proc Natl Acad Sci U S A 99: 6679-6683.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 6679-6683
    • Mihara, H.1    Kato, S.2    Lacourciere, G.M.3    Stadtman, T.C.4    Kennedy, R.A.5
  • 30
    • 9244265496 scopus 로고    scopus 로고
    • Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling L-selenocysteine and Sps2 for selenite assimilation
    • Tamura T, Yamamoto S, Takahata M, Sakaguchi H, Tanaka H, et al. (2004) Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling L-selenocysteine and Sps2 for selenite assimilation. Proc Natl Acad Sci U S A 101: 16162-16167.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 16162-16167
    • Tamura, T.1    Yamamoto, S.2    Takahata, M.3    Sakaguchi, H.4    Tanaka, H.5
  • 31
    • 12844265308 scopus 로고    scopus 로고
    • Characterization of potential selenium-binding proteins in the selenophosphate synthetase system
    • Ogasawara Y, Lacourciere GM, Ishii K, Stadtman TC, (2005) Characterization of potential selenium-binding proteins in the selenophosphate synthetase system. Proc Natl Acad Sci U S A 102: 1012-1016.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 1012-1016
    • Ogasawara, Y.1    Lacourciere, G.M.2    Ishii, K.3    Stadtman, T.C.4
  • 32
    • 77951215521 scopus 로고    scopus 로고
    • Reaction mechanism and molecular basis for selenium/sulfur discrimination of selenocysteine lyase
    • Omi R, Kurokawa S, Mihara H, Hayashi H, Goto M, et al. (2010) Reaction mechanism and molecular basis for selenium/sulfur discrimination of selenocysteine lyase. J Biol Chem 285: 12133-12139.
    • (2010) J Biol Chem , vol.285 , pp. 12133-12139
    • Omi, R.1    Kurokawa, S.2    Mihara, H.3    Hayashi, H.4    Goto, M.5
  • 33
    • 0343851637 scopus 로고    scopus 로고
    • The manifold of vitamin B6 dependent enzymes
    • Schneider G, Kack H, Lindqvist Y, (2000) The manifold of vitamin B6 dependent enzymes. Structure 8: R1-6.
    • (2000) Structure , vol.8
    • Schneider, G.1    Kack, H.2    Lindqvist, Y.3
  • 34
    • 84861741119 scopus 로고    scopus 로고
    • Biochemical discrimination between selenium and sulfur 2: Mechanistic investigation of the selenium specificity of human selenocysteine lyase
    • In press
    • Johansson A-L, Collins R, Arnér ESJ, Brzezinski P, Högbom M, (2012) Biochemical discrimination between selenium and sulfur 2: Mechanistic investigation of the selenium specificity of human selenocysteine lyase. PLoS ONE In press.
    • (2012) PLoS ONE
    • Johansson, A.-L.1    Collins, R.2    Arnér, E.S.J.3    Brzezinski, P.4    Högbom, M.5
  • 35
    • 0031570320 scopus 로고    scopus 로고
    • Selenophosphate synthetase: enzyme labeling studies with [gamma-32P]ATP, [beta-32P]ATP, [8-14C]ATP, and [75Se]selenide
    • Liu SY, Stadtman TC, (1997) Selenophosphate synthetase: enzyme labeling studies with [gamma-32P]ATP, [beta-32P]ATP, [8-14C]ATP, and [75Se]selenide. Arch Biochem Biophys 341: 353-359.
    • (1997) Arch Biochem Biophys , vol.341 , pp. 353-359
    • Liu, S.Y.1    Stadtman, T.C.2
  • 36
    • 58549089314 scopus 로고    scopus 로고
    • Structure of selenophosphate synthetase essential for selenium incorporation into proteins and RNAs
    • Itoh Y, Sekine S, Matsumoto E, Akasaka R, Takemoto C, et al. (2009) Structure of selenophosphate synthetase essential for selenium incorporation into proteins and RNAs. J Mol Biol 385: 1456-1469.
    • (2009) J Mol Biol , vol.385 , pp. 1456-1469
    • Itoh, Y.1    Sekine, S.2    Matsumoto, E.3    Akasaka, R.4    Takemoto, C.5
  • 37
    • 67049155897 scopus 로고    scopus 로고
    • Identification of proteins interacting with selenocysteine lyase
    • Tobe R, Mihara H, Kurihara T, Esaki N, (2009) Identification of proteins interacting with selenocysteine lyase. Biosci Biotechnol Biochem 73: 1230-1232.
    • (2009) Biosci Biotechnol Biochem , vol.73 , pp. 1230-1232
    • Tobe, R.1    Mihara, H.2    Kurihara, T.3    Esaki, N.4
  • 38
    • 34249005313 scopus 로고    scopus 로고
    • Selenophosphate synthetase 2 is essential for selenoprotein biosynthesis
    • Xu XM, Carlson BA, Irons R, Mix H, Zhong N, et al. (2007) Selenophosphate synthetase 2 is essential for selenoprotein biosynthesis. Biochem J 404: 115-20.
    • (2007) Biochem J , vol.404 , pp. 115-120
    • Xu, X.M.1    Carlson, B.A.2    Irons, R.3    Mix, H.4    Zhong, N.5
  • 39
    • 37549018459 scopus 로고    scopus 로고
    • Selenoproteinless animals: selenophosphate synthetase SPS1 functions in a pathway unrelated to selenocysteine biosynthesis
    • Lobanov AV, Hatfield DL, Gladyshev VN, (2008) Selenoproteinless animals: selenophosphate synthetase SPS1 functions in a pathway unrelated to selenocysteine biosynthesis. Protein Sci 17: 176-82.
    • (2008) Protein Sci , vol.17 , pp. 176-182
    • Lobanov, A.V.1    Hatfield, D.L.2    Gladyshev, V.N.3
  • 40
  • 41
    • 0027879008 scopus 로고
    • Automatic Processing of Rotation Diffraction Data from Crystals of Initially Unknown Symmetry and Cell Constants
    • Kabsch W, (1993) Automatic Processing of Rotation Diffraction Data from Crystals of Initially Unknown Symmetry and Cell Constants. J Appl Cryst 26: 795-800.
    • (1993) J Appl Cryst , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 42
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ, (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst D 53: 240-255.
    • (1997) Acta Cryst D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 43
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 44
    • 0000243829 scopus 로고
    • Procheck - A Program to Check the Stereochemical Quality of Protein Structures
    • Laskowski RA, Macarthur MW, Moss DS, Thornton JM, (1993) Procheck- A Program to Check the Stereochemical Quality of Protein Structures. J Appl Cryst 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


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