메뉴 건너뛰기




Volumn 7, Issue 1, 2012, Pages

Biochemical discrimination between selenium and sulfur 2: Mechanistic investigation of the selenium specificity of human selenocysteine lyase

Author keywords

[No Author keywords available]

Indexed keywords

LYASE; SELENIUM; SELENOCYSTEINE LYASE; SULFUR; UNCLASSIFIED DRUG; SELENOCYSTEINE;

EID: 84861741119     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0030528     Document Type: Article
Times cited : (14)

References (34)
  • 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
  • 3
    • 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
  • 4
    • 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
  • 5
    • 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
  • 7
    • 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
  • 8
    • 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
  • 9
    • 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
  • 11
    • 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
  • 12
    • 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
  • 13
    • 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
  • 14
    • 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
  • 15
    • 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
  • 16
    • 0028265941 scopus 로고
    • Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product
    • Zheng L, White RH, Cash VL, Dean DR, (1994) Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product. Biochemistry 33: 4714-4720.
    • (1994) Biochemistry , vol.33 , pp. 4714-4720
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Dean, D.R.4
  • 17
    • 0034708346 scopus 로고    scopus 로고
    • Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulphur cluster assembly
    • Kaiser JT, Clausen T, Bourenkow GP, Bartunik HD, Steinbacher S, et al. (2000) Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulphur cluster assembly. J Mol Biol 297: 451-464.
    • (2000) J Mol Biol , vol.297 , pp. 451-464
    • Kaiser, J.T.1    Clausen, T.2    Bourenkow, G.P.3    Bartunik, H.D.4    Steinbacher, S.5
  • 18
    • 0347997282 scopus 로고    scopus 로고
    • Snapshots of the cystine lyase C-DES during catalysis. Studies in solution and in the crystalline state
    • Kaiser JT, Bruno S, Clausen T, Huber R, Schiaretti F, et al. (2003) Snapshots of the cystine lyase C-DES during catalysis. Studies in solution and in the crystalline state. J Biol Chem 278: 357-365.
    • (2003) J Biol Chem , vol.278 , pp. 357-365
    • Kaiser, J.T.1    Bruno, S.2    Clausen, T.3    Huber, R.4    Schiaretti, F.5
  • 19
    • 33846020960 scopus 로고    scopus 로고
    • Sulfur mobilization in cyanobacteria: the catalytic mechanism of L-cystine C-S lyase (C-DES) from synechocystis
    • Campanini B, Schiaretti F, Abbruzzetti S, Kessler D, Mozzarelli A, (2006) Sulfur mobilization in cyanobacteria: the catalytic mechanism of L-cystine C-S lyase (C-DES) from synechocystis. J Biol Chem 281: 38769-38780.
    • (2006) J Biol Chem , vol.281 , pp. 38769-38780
    • Campanini, B.1    Schiaretti, F.2    Abbruzzetti, S.3    Kessler, D.4    Mozzarelli, A.5
  • 20
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis
    • Zheng L, White RH, Cash VL, Jack RF, Dean DR, (1993) Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis. Proc Natl Acad Sci U S A 90: 2754-2758.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 2754-2758
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Jack, R.F.4    Dean, D.R.5
  • 21
    • 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
  • 22
    • 0036562516 scopus 로고    scopus 로고
    • Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: implications for its specificity toward selenocysteine
    • Mihara H, Fujii T, Kato S, Kurihara T, Hata Y, et al. (2002) Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: implications for its specificity toward selenocysteine. J Biochem (Tokyo) 131: 679-685.
    • (2002) J Biochem (Tokyo) , vol.131 , pp. 679-685
    • Mihara, H.1    Fujii, T.2    Kato, S.3    Kurihara, T.4    Hata, Y.5
  • 23
    • 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
  • 24
    • 4644301523 scopus 로고    scopus 로고
    • Mechanism of cysteine desulfurase Slr0387 from Synechocystis sp. PCC 6803: kinetic analysis of cleavage of the persulfide intermediate by chemical reductants
    • Behshad E, Parkin SE, Bollinger JM Jr, (2004) Mechanism of cysteine desulfurase Slr0387 from Synechocystis sp. PCC 6803: kinetic analysis of cleavage of the persulfide intermediate by chemical reductants. Biochemistry 43: 12220-12226.
    • (2004) Biochemistry , vol.43 , pp. 12220-12226
    • Behshad, E.1    Parkin, S.E.2    Bollinger Jr., J.M.3
  • 25
    • 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
  • 26
    • 84861954783 scopus 로고    scopus 로고
    • Biochemical discrimination between selenium and sulfur 1: A single residue provides selenium specificity to human selenocysteine lyase
    • In press
    • Collins R, Johansson A-L, Karlberg T, Markova N, van den Berg S, et al. (2012) Biochemical discrimination between selenium and sulfur 1: A single residue provides selenium specificity to human selenocysteine lyase. PLoS ONE In press.
    • (2012) PLoS ONE
    • Collins, R.1    Johansson, A.-L.2    Karlberg, T.3    Markova, N.4    van den Berg, S.5
  • 27
    • 0033591390 scopus 로고    scopus 로고
    • A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase. Gene cloning, purification, characterization and preliminary x-ray crystallographic studies
    • Mihara H, Maeda M, Fujii T, Kurihara T, Hata Y, et al. (1999) A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase. Gene cloning, purification, characterization and preliminary x-ray crystallographic studies. J Biol Chem 274: 14768-14772.
    • (1999) J Biol Chem , vol.274 , pp. 14768-14772
    • Mihara, H.1    Maeda, M.2    Fujii, T.3    Kurihara, T.4    Hata, Y.5
  • 29
    • 72449186508 scopus 로고    scopus 로고
    • Kinetic analysis of cysteine desulfurase CD0387 from Synechocystis sp. PCC 6803: formation of the persulfide intermediate
    • Behshad E, Bollinger JM Jr, (2009) Kinetic analysis of cysteine desulfurase CD0387 from Synechocystis sp. PCC 6803: formation of the persulfide intermediate. Biochemistry 48: 12014-12023.
    • (2009) Biochemistry , vol.48 , pp. 12014-12023
    • Behshad, E.1    Bollinger Jr., J.M.2
  • 30
    • 4644275046 scopus 로고    scopus 로고
    • Kinetic and structural characterization of Slr0077/SufS, the essential cysteine desulfurase from Synechocystis sp. PCC 6803
    • Tirupati B, Vey JL, Drennan CL, Bollinger JM Jr, (2004) Kinetic and structural characterization of Slr0077/SufS, the essential cysteine desulfurase from Synechocystis sp. PCC 6803. Biochemistry 43: 12210-12219.
    • (2004) Biochemistry , vol.43 , pp. 12210-12219
    • Tirupati, B.1    Vey, J.L.2    Drennan, C.L.3    Bollinger Jr., J.M.4
  • 31
    • 0036945691 scopus 로고    scopus 로고
    • The role of ate complexes in the lithium-sulfur, lithium-selenium and lithium-tellurium exchange reactions
    • Reich HJ, Gudmundsson BO, Green DP, Bevan MJ, Reich IL, (2002) The role of ate complexes in the lithium-sulfur, lithium-selenium and lithium-tellurium exchange reactions. Helvetica Chimica Acta 85: 3748-3772.
    • (2002) Helvetica Chimica Acta , vol.85 , pp. 3748-3772
    • Reich, H.J.1    Gudmundsson, B.O.2    Green, D.P.3    Bevan, M.J.4    Reich, I.L.5
  • 32
    • 84981477933 scopus 로고
    • Alpha-Heterosubstituted Organyllithium Compounds by Selenium-Lithium-Exchange - Directed Coupling of Carbonyl-Compounds
    • Seebach D, Meyer N, Beck AK, (1977) Alpha-Heterosubstituted Organyllithium Compounds by Selenium-Lithium-Exchange- Directed Coupling of Carbonyl-Compounds. Justus Liebigs Annalen Der Chemie pp. 846-858.
    • (1977) Justus Liebigs Annalen Der Chemie , pp. 846-858
    • Seebach, D.1    Meyer, N.2    Beck, A.K.3
  • 33
    • 77952563903 scopus 로고    scopus 로고
    • Selenoproteins-What unique properties can arise with selenocysteine in place of cysteine?
    • Arner ES, (2010) Selenoproteins-What unique properties can arise with selenocysteine in place of cysteine? Exp Cell Res 316: 1296-1303.
    • (2010) Exp Cell Res , vol.316 , pp. 1296-1303
    • Arner, E.S.1
  • 34
    • 79959345933 scopus 로고    scopus 로고
    • Differing views of the role of selenium in thioredoxin reductase
    • Hondal RJ, Ruggles EL, (2011) Differing views of the role of selenium in thioredoxin reductase. Amino Acids 41: 73-89.
    • (2011) Amino Acids , vol.41 , pp. 73-89
    • Hondal, R.J.1    Ruggles, E.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.