메뉴 건너뛰기




Volumn 287, Issue 3, 2012, Pages 1688-1697

Structural and mechanistic insights into unusual thiol disulfide oxidoreductase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; CATALYTIC MECHANISMS; CONSENSUS SEQUENCE; DESULFOVIBRIO VULGARIS; DISULFIDE REDUCTASE; GAIN INSIGHT; HISTIDINE RESIDUES; ISOMERASE ACTIVITY; MOLECULAR MECHANISM; NEW MEMBERS; NMR STRUCTURES; OXIDIZED STATE; OXIDOREDUCTASES; PH DEPENDENCE; REDOX POTENTIALS; REDOX STATE; REDUCED-STATE; THIOL GROUPS; THIOL-DISULFIDE; THIOREDOXINS;

EID: 84855860396     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.288316     Document Type: Article
Times cited : (5)

References (35)
  • 1
    • 0029187491 scopus 로고
    • Thioredoxin and thioredoxin reductase
    • Holmgren, A., and Björnstedt, M. (1995) Thioredoxin and thioredoxin reductase. Methods Enzymol. 252, 199-208
    • (1995) Methods Enzymol. , vol.252 , pp. 199-208
    • Holmgren, A.1    Björnstedt, M.2
  • 2
    • 0032411723 scopus 로고    scopus 로고
    • The genetics of disulfide bond metabolism
    • DOI 10.1146/annurev.genet.32.1.163
    • Rietsch, A., and Beckwith, J. (1998) The genetics of disulfide bond metabolism. Annu. Rev. Genet 32, 163-184 (Pubitemid 29045311)
    • (1998) Annual Review of Genetics , vol.32 , pp. 163-184
    • Rietsch, A.1    Beckwith, J.2
  • 3
    • 0029165589 scopus 로고
    • Thioredoxin: A fold for all reasons
    • Martin, J. L. (1995) Thioredoxin: a fold for all reasons. Structure 3, 245-250
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 4
    • 0039714219 scopus 로고    scopus 로고
    • Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases
    • Mössner, E., Huber-Wunderlich, M., and Glockshuber, R. (1998) Characterization of Escherichia coli thioredoxin variants mimicking the activesites of other thiol/disulfide oxidoreductases. Protein Sci. 7, 1233-1244 (Pubitemid 28237057)
    • (1998) Protein Science , vol.7 , Issue.5 , pp. 1233-1244
    • Mossner, E.1    Huber-Wunderlich, M.2    Glockshuber, R.3
  • 5
    • 0030695902 scopus 로고    scopus 로고
    • Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein- protein redox equilibria
    • DOI 10.1074/jbc.272.49.30780
    • Aslund, F., Berndt, K. D., and Holmgren, A. (1997) Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria. J. Biol. Chem. 272, 30780-30786 (Pubitemid 27527515)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.49 , pp. 30780-30786
    • Aslund, F.1    Berndt, K.D.2    Holmgren, A.3
  • 6
    • 77956514975 scopus 로고    scopus 로고
    • The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1α
    • Chambers, J. E., Tavender, T. J., Oka, O. B., Warwood, S., Knight, D., and Bulleid, N. J. (2010) The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1α. J. Biol. Chem. 285, 29200-29207
    • (2010) J. Biol. Chem. , vol.285 , pp. 29200-29207
    • Chambers, J.E.1    Tavender, T.J.2    Oka, O.B.3    Warwood, S.4    Knight, D.5    Bulleid, N.J.6
  • 7
    • 0037533415 scopus 로고    scopus 로고
    • Catalysis of protein folding by protein disulfide isomerase and small-molecule mimics
    • Kersteen, E. A., and Raines, R. T. (2003) Catalysis of protein folding by protein disulfide isomerase and small-molecule mimics. Antioxid. Redox Signal. 5, 413-424 (Pubitemid 37087401)
    • (2003) Antioxidants and Redox Signaling , vol.5 , Issue.4 , pp. 413-424
    • Kersteen, E.A.1    Raines, R.T.2
  • 9
    • 0035979799 scopus 로고    scopus 로고
    • Structure of the soluble domain of a membrane-anchored thioredoxin-like protein from Bradyrhizobium japonicum reveals unusual properties
    • DOI 10.1006/jmbi.2001.4913
    • Capitani, G., Rossmann, R., Sargent, D. F., Grütter, M. G., Richmond, T. J., and Hennecke, H. (2001) Structure of the soluble domain of a membraneanchored thioredoxin-like protein from Bradyrhizobium japonicum reveals unusual properties. J. Mol. Biol. 311, 1037-1048 (Pubitemid 32803719)
    • (2001) Journal of Molecular Biology , vol.311 , Issue.5 , pp. 1037-1048
    • Capitani, G.1    Rossmann, R.2    Sargent, D.F.3    Grutter, M.G.4    Richmond, T.J.5    Hennecke, H.6
  • 11
    • 0029057023 scopus 로고
    • Proton sharing between cysteine thiols in Escherichia coli thioredoxin: Implications for the mechanism of protein disulfide reduction
    • Jeng, M. F., Holmgren, A., and Dyson, H. J. (1995) Proton sharing between cysteine thiols in Escherichia coli thioredoxin: implications for the mechanism of protein disulfide reduction. Biochemistry 34, 10101-10105
    • (1995) Biochemistry , vol.34 , pp. 10101-10105
    • Jeng, M.F.1    Holmgren, A.2    Dyson, H.J.3
  • 12
    • 40549093328 scopus 로고    scopus 로고
    • Mechanism of thioredoxin-catalyzed disulfide reduction. Activation of the buried thiol and role of the variable active-site residues
    • DOI 10.1021/jp7104665
    • Carvalho, A. T., Swart, M., van Stralen, J. N., Fernandes, P. A., Ramos, M. J., and Bickelhaupt, F. M. (2008) Mechanism of thioredoxin-catalyzed disulfide reduction: activation of the buried thiol and role of the variable activesite residues. J. Phys. Chem. B 112, 2511-2523 (Pubitemid 351362374)
    • (2008) Journal of Physical Chemistry B , vol.112 , Issue.8 , pp. 2511-2523
    • Carvalho, A.T.P.1    Swart, M.2    Van Straten, J.N.P.3    Fernandes, P.A.4    Ramos, M.J.5    Bickelhaupt, F.M.6
  • 14
    • 79953158381 scopus 로고    scopus 로고
    • Study of the thiol/disulfide redox systems of the anaerobe Desulfovibrio vulgaris points out pyruvate:ferredoxin oxidoreductase as a new target for thioredoxin 1
    • Pieulle, L., Stocker, P., Vinay, M., Nouailler, M., Vita, N., Brasseur, G., Garcin, E., Sebban-Kreuzer, C., and Dolla, A. (2011) Study of the thiol/disulfide redox systems of the anaerobe Desulfovibrio vulgaris points out pyruvate:ferredoxin oxidoreductase as a new target for thioredoxin 1. J. Biol. Chem. 286, 7812-7821
    • (2011) J. Biol. Chem. , vol.286 , pp. 7812-7821
    • Pieulle, L.1    Stocker, P.2    Vinay, M.3    Nouailler, M.4    Vita, N.5    Brasseur, G.6    Garcin, E.7    Sebban-Kreuzer, C.8    Dolla, A.9
  • 16
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren, A. (1979) Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J. Biol. Chem. 254, 9627-9632
    • (1979) J. Biol. Chem. , vol.254 , pp. 9627-9632
    • Holmgren, A.1
  • 17
    • 0021152329 scopus 로고
    • Formation and isomerization of disulfide bonds in proteins: Protein disulfide-isomerase
    • Hillson, D. A., Lambert, N., and Freedman, R. B. (1984) Formation and isomerization of disulfide bonds in proteins: protein disulfide-isomerase. Methods Enzymol. 107, 281-294
    • (1984) Methods Enzymol. , vol.107 , pp. 281-294
    • Hillson, D.A.1    Lambert, N.2    Freedman, R.B.3
  • 19
    • 0030059821 scopus 로고    scopus 로고
    • Direct measurement of the aspartic acid 26 pKa for reduced Escherichia coli thioredoxin by 13C NMR
    • Jeng, M. F., and Dyson, H. J. (1996) Direct measurement of the aspartic acid 26 pKa for reduced Escherichia coli thioredoxin by 13C NMR. Biochemistry 35, 1-6
    • (1996) Biochemistry , vol.35 , pp. 1-6
    • Jeng, M.F.1    Dyson, H.J.2
  • 21
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • DOI 10.1023/A:1008392405740
    • Cornilescu, G., Delaglio, F., and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289-302 (Pubitemid 29143535)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.3 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 23
    • 54349105625 scopus 로고    scopus 로고
    • Heterologous expression of lipase in Escherichia coli is limited by folding and disulfide bond formation
    • Xu, Y., Yasin, A., Tang, R., Scharer, J. M., Moo-Young, M., and Chou, C. P. (2008) Heterologous expression of lipase in Escherichia coli is limited by folding and disulfide bond formation. Appl. Microbiol. Biotechnol. 81, 79-87
    • (2008) Appl. Microbiol. Biotechnol. , vol.81 , pp. 79-87
    • Xu, Y.1    Yasin, A.2    Tang, R.3    Scharer, J.M.4    Moo-Young, M.5    Chou, C.P.6
  • 24
    • 65249146593 scopus 로고    scopus 로고
    • Structural and biochemical characterization of Xylella fastidiosa DsbA family members: New insights into the enzyme-substrate interaction
    • Rinaldi, F. C., Meza, A. N., and Guimarães, B. G. (2009) Structural and biochemical characterization of Xylella fastidiosa DsbA family members: new insights into the enzyme-substrate interaction. Biochemistry 48, 3508-3518
    • (2009) Biochemistry , vol.48 , pp. 3508-3518
    • Rinaldi, F.C.1    Meza, A.N.2    Guimarães, B.G.3
  • 25
    • 0025914427 scopus 로고
    • Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin
    • Krause, G., Lundström, J., Barea, J. L., Pueyo de la Cuesta, C., and Holmgren, A. (1991) Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin. J. Biol. Chem. 266, 9494-9500 (Pubitemid 21906684)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.15 , pp. 9494-9500
    • Krause, G.1    Lundstrom, J.2    Barea, J.L.3    De La, C.C.P.4    Holmgren, A.5
  • 26
    • 0027481123 scopus 로고
    • Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli
    • Wunderlich, M., and Glockshuber, R. (1993) Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli. Protein Sci. 2, 717-726 (Pubitemid 23121086)
    • (1993) Protein Science , vol.2 , Issue.5 , pp. 717-726
    • Wunderlich, M.1    Glockshuber, R.2
  • 27
    • 0027293791 scopus 로고
    • Determination of the reduction-oxidation potential of the thioredoxin- like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin
    • Lundström, J., and Holmgren, A. (1993) Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin. Biochemistry 32, 6649-6655 (Pubitemid 23217134)
    • (1993) Biochemistry , vol.32 , Issue.26 , pp. 6649-6655
    • Lundstrom, J.1    Holmgren, A.2
  • 28
    • 0029559184 scopus 로고
    • Why is DsbA such an oxidizing disulfide catalyst?
    • DOI 10.1016/0092-8674(95)90210-4
    • Grauschopf, U., Winther, J. R., Korber, P., Zander, T., Dallinger, P., and Bardwell, J. C. (1995) Why is DsbA such an oxidizing disulfide catalyst? Cell 83, 947-955 (Pubitemid 26006536)
    • (1995) Cell , vol.83 , Issue.6 , pp. 947-955
    • Grauschopf, U.1    Winther, J.R.2    Korber, P.3    Zander, T.4    Dallinger, P.5    Bardwell, J.C.A.6
  • 29
    • 33748331135 scopus 로고    scopus 로고
    • Protein disulfides and protein disulfide oxidoreductases in hyperthermophiles
    • DOI 10.1111/j.1742-4658.2006.05421.x
    • Ladenstein, R., and Ren, B. (2006) Protein disulfides and protein disulfide oxidoreductases in hyperthermophiles. FEBS J. 273, 4170-4185 (Pubitemid 44326498)
    • (2006) FEBS Journal , vol.273 , Issue.18 , pp. 4170-4185
    • Ladenstein, R.1    Ren, B.2
  • 30
    • 0348230942 scopus 로고    scopus 로고
    • Glutaredoxins: Glutathione-Dependent Redox Enzymes with Functions Far Beyond a Simple Thioredoxin Backup System
    • Fernandes, A. P., and Holmgren, A. (2004) Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Antioxid. Redox. Signal. 6, 63-74 (Pubitemid 38063976)
    • (2004) Antioxidants and Redox Signaling , vol.6 , Issue.1 , pp. 63-74
    • Fernandes, A.P.1    Holmgren, A.2
  • 32
    • 0031442195 scopus 로고    scopus 로고
    • General acid/base catalysis in the active site of Escherichia coli thioredoxin
    • DOI 10.1021/bi971504l
    • Chivers, P. T., and Raines, R. T. (1997) General acid/base catalysis in the active site of Escherichia coli thioredoxin. Biochemistry 36, 15810-15816 (Pubitemid 28027381)
    • (1997) Biochemistry , vol.36 , Issue.50 , pp. 15810-15816
    • Chivers, P.T.1    Raines, R.T.2
  • 33
    • 33646560034 scopus 로고    scopus 로고
    • Determination of the DeltapKa between the active site cysteines of thioredoxin and DsbA
    • DOI 10.1002/jcc.20404
    • Carvalho, A. T., Fernandes, P. A., and Ramos, M. J. (2006) Determination of the DeltapKa between the active site cysteines of thioredoxin and DsbA. J. Comput. Chem. 27, 966-975 (Pubitemid 43723219)
    • (2006) Journal of Computational Chemistry , vol.27 , Issue.8 , pp. 966-975
    • Carvalho, A.T.P.1    Fernandes, P.A.2    Ramos, M.J.3
  • 34
    • 77956318615 scopus 로고    scopus 로고
    • Mechanisms of oxidative protein folding in the bacterial cell envelope
    • Kadokura, H., and Beckwith, J. (2010) Mechanisms of oxidative protein folding in the bacterial cell envelope. Antioxid. Redox Signal. 13, 1231-1246
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1231-1246
    • Kadokura, H.1    Beckwith, J.2
  • 35
    • 0030880594 scopus 로고    scopus 로고
    • Structural analysis of three His32 mutants of DsbA: Support for an electrostatic role of His32 in DsbA stability
    • Guddat, L. W., Bardwell, J. C., Glockshuber, R., Huber-Wunderlich, M., Zander, T., and Martin, J. L. (1997) Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability. Protein Sci. 6, 1893-1900 (Pubitemid 27391270)
    • (1997) Protein Science , vol.6 , Issue.9 , pp. 1893-1900
    • Guddat, L.W.1    Bardwell, J.C.A.2    Glockshuber, R.3    Huber-Wunderlich, M.4    Zander, T.5    Martin, J.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.