메뉴 건너뛰기




Volumn 47, Issue 17, 2008, Pages 4955-4963

Human quiescin-sulfhydryl oxidase, QSOX1: Probing internal redox steps by mutagenesis

Author keywords

[No Author keywords available]

Indexed keywords

CONCOMITANT REDUCTION; QUIESCIN SULFHYDRYL OXIDASE; THIOREDOXINS;

EID: 42449098493     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi702522q     Document Type: Article
Times cited : (75)

References (48)
  • 2
    • 0141765887 scopus 로고    scopus 로고
    • Avian sulftiydryl oxidase is not a metalloenzyme: Adventitious binding of divalent metal ions to the enzyme
    • Brohawn, S. G., Rudik, I., and Thorpe, C. (2003) Avian sulftiydryl oxidase is not a metalloenzyme: adventitious binding of divalent metal ions to the enzyme. Biochemistry 42, 11074-11082.
    • (2003) Biochemistry , vol.42 , pp. 11074-11082
    • Brohawn, S.G.1    Rudik, I.2    Thorpe, C.3
  • 3
    • 34347204504 scopus 로고    scopus 로고
    • Generating disulfides in multicellular organisms: Emerging roles for a new flavoprotein family
    • Thorpe, C., and Coppock, D. L. (2007) Generating disulfides in multicellular organisms: Emerging roles for a new flavoprotein family. J. Biol. Chem. 282, 13929-13933.
    • (2007) J. Biol. Chem , vol.282 , pp. 13929-13933
    • Thorpe, C.1    Coppock, D.L.2
  • 4
    • 33646688670 scopus 로고    scopus 로고
    • Multidomain flavin-dependent sulfhydryl oxidases
    • Coppock, D. L., and Thorpe, C. (2006) Multidomain flavin-dependent sulfhydryl oxidases. Antioxid. Redox Signal. 8, 300-311.
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 300-311
    • Coppock, D.L.1    Thorpe, C.2
  • 5
    • 0034647976 scopus 로고    scopus 로고
    • Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase
    • Lee, J., Hofhaus, G., and Lisowsky, T. (2000) Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase. FEBS Lett. 477 (1-2), 62-66.
    • (2000) FEBS Lett , vol.477 , Issue.1-2 , pp. 62-66
    • Lee, J.1    Hofhaus, G.2    Lisowsky, T.3
  • 6
    • 0035968186 scopus 로고    scopus 로고
    • Yeast ERV2p is the first microsomal FAD-linked sulfhydryl oxidase of the Erv1p/Alrp protein family
    • Gerber, J., Muhlenhoff, U., Hofhaus, G., Lill, R., and Lisowsky, T. (2001) Yeast ERV2p is the first microsomal FAD-linked sulfhydryl oxidase of the Erv1p/Alrp protein family. J. Biol. Chem. 276, 23486-23491.
    • (2001) J. Biol. Chem , vol.276 , pp. 23486-23491
    • Gerber, J.1    Muhlenhoff, U.2    Hofhaus, G.3    Lill, R.4    Lisowsky, T.5
  • 7
    • 0036142325 scopus 로고    scopus 로고
    • A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p
    • Gross, E., Sevier, C. S., Vala, A., Kaiser, C. A., and Fass, D. (2002) A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nat. Struct. Biol. 9, 61-67.
    • (2002) Nat. Struct. Biol , vol.9 , pp. 61-67
    • Gross, E.1    Sevier, C.S.2    Vala, A.3    Kaiser, C.A.4    Fass, D.5
  • 8
    • 0034790475 scopus 로고    scopus 로고
    • A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation
    • Sevier, C. S., Cuozzo, J. W., Vala, A., Aslund, F., and Kaiser, C. A. (2001) A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation. Nat. Cell Biol. 3, 874-882.
    • (2001) Nat. Cell Biol , vol.3 , pp. 874-882
    • Sevier, C.S.1    Cuozzo, J.W.2    Vala, A.3    Aslund, F.4    Kaiser, C.A.5
  • 9
    • 0037407929 scopus 로고    scopus 로고
    • The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase
    • Wu, C. K., Dailey, T. A., Dailey, H. A., Wang, B. C., and Rose, J. P. (2003) The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase. Protein Sci. 12, 1109-1118.
    • (2003) Protein Sci , vol.12 , pp. 1109-1118
    • Wu, C.K.1    Dailey, T.A.2    Dailey, H.A.3    Wang, B.C.4    Rose, J.P.5
  • 10
    • 13444304104 scopus 로고    scopus 로고
    • Augmenter of liver regeneration: A flavin dependent sulfhydryl oxidase with cytochrome C reductase activity
    • Farrell, S. R., and Thorpe, C. (2005) Augmenter of liver regeneration: a flavin dependent sulfhydryl oxidase with cytochrome C reductase activity. Biochemistry 44, 1532-1541.
    • (2005) Biochemistry , vol.44 , pp. 1532-1541
    • Farrell, S.R.1    Thorpe, C.2
  • 11
    • 1542467584 scopus 로고    scopus 로고
    • The potentiation role of hepatopoietin on activator protein-1 is dependent on its sulfhydryl oxidase activity
    • Chen, X., Li, Y., Wei, K., Li, L., Liu, W., Zhu, Y., Qiu, Z., and He, F. (2003) The potentiation role of hepatopoietin on activator protein-1 is dependent on its sulfhydryl oxidase activity. J. Biol. Chem. 278, 49022-49030.
    • (2003) J. Biol. Chem , vol.278 , pp. 49022-49030
    • Chen, X.1    Li, Y.2    Wei, K.3    Li, L.4    Liu, W.5    Zhu, Y.6    Qiu, Z.7    He, F.8
  • 12
    • 2442567796 scopus 로고    scopus 로고
    • Unique features of plant mitochondrial sulfhydryl oxidase
    • Levitan, A., Danon, A., and Lisowsky, T. (2004) Unique features of plant mitochondrial sulfhydryl oxidase. J. Biol. Chem. 279, 20002-20008.
    • (2004) J. Biol. Chem , vol.279 , pp. 20002-20008
    • Levitan, A.1    Danon, A.2    Lisowsky, T.3
  • 13
    • 33747352990 scopus 로고    scopus 로고
    • Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide
    • Vitu, E., Bentzur, M., Lisowsky, T., Kaiser, C. A., and Fass, D. (2006) Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide. J. Mol. Biol. 362, 89-101.
    • (2006) J. Mol. Biol , vol.362 , pp. 89-101
    • Vitu, E.1    Bentzur, M.2    Lisowsky, T.3    Kaiser, C.A.4    Fass, D.5
  • 14
    • 0037076339 scopus 로고    scopus 로고
    • Complete pathway for protein disulfide bond formation encoded by poxviruses
    • Senkevich, T. G., White, C. L., Koonin, E. V., and Moss, B. (2002) Complete pathway for protein disulfide bond formation encoded by poxviruses. Proc. Natl. Acad. Sci. U.S.A. 99, 6667-6672.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 6667-6672
    • Senkevich, T.G.1    White, C.L.2    Koonin, E.V.3    Moss, B.4
  • 15
    • 33645239489 scopus 로고    scopus 로고
    • African swine fever virus pB119L protein is a flavin adenine dinucleotide-linked sulfhydryl oxidase
    • Rodriguez, I., Redrejo-Rodriguez, M., Rodriguez, J. M., Alejo, A., Salas, J., and Salas, M. L. (2006) African swine fever virus pB119L protein is a flavin adenine dinucleotide-linked sulfhydryl oxidase. J. Virol. 80, 3157-3166.
    • (2006) J. Virol , vol.80 , pp. 3157-3166
    • Rodriguez, I.1    Redrejo-Rodriguez, M.2    Rodriguez, J.M.3    Alejo, A.4    Salas, J.5    Salas, M.L.6
  • 16
    • 42449137700 scopus 로고    scopus 로고
    • Heckler, E. J., Rancy, P. C., Kodali, V. K., and Thorpe, C. (2007) Generating disulfides with the quiescin sulfhydryl oxidases, Biochim. Biophys. Acta, Epub ahead of print.
    • Heckler, E. J., Rancy, P. C., Kodali, V. K., and Thorpe, C. (2007) Generating disulfides with the quiescin sulfhydryl oxidases, Biochim. Biophys. Acta, Epub ahead of print.
  • 17
    • 0037461350 scopus 로고    scopus 로고
    • Inter-domain redox communication in flavoenzymes of the quiescin/sulfhydryl oxidase family: Role of a thioredoxin domain in disulfide bond formation
    • Raje, S., and Thorpe, C. (2003) Inter-domain redox communication in flavoenzymes of the quiescin/sulfhydryl oxidase family: role of a thioredoxin domain in disulfide bond formation. Biochemistry 42, 4560-4568.
    • (2003) Biochemistry , vol.42 , pp. 4560-4568
    • Raje, S.1    Thorpe, C.2
  • 18
    • 0019321282 scopus 로고
    • Properties of a flavoprotein sulfhydryl oxidase from rat seminal vesicle secretion
    • Ostrowski, M. C., and Kistler, W. S. (1980) Properties of a flavoprotein sulfhydryl oxidase from rat seminal vesicle secretion. Biochemistry 19, 2639-2645.
    • (1980) Biochemistry , vol.19 , pp. 2639-2645
    • Ostrowski, M.C.1    Kistler, W.S.2
  • 19
  • 20
    • 0033529555 scopus 로고    scopus 로고
    • Sulfhydryl oxidase from egg white: A facile catalyst for disulfide bond formation in proteins and peptides
    • Hoober, K. L., Sheasley, S. S., Gilbert, H. F., and Thorpe, C. (1999) Sulfhydryl oxidase from egg white: a facile catalyst for disulfide bond formation in proteins and peptides. J. Biol. Chem. 274, 22147-22150.
    • (1999) J. Biol. Chem , vol.274 , pp. 22147-22150
    • Hoober, K.L.1    Sheasley, S.S.2    Gilbert, H.F.3    Thorpe, C.4
  • 21
    • 0033537679 scopus 로고    scopus 로고
    • Egg white sulfhydryl oxidase: Kinetic mechanism of the catalysis of disulfide bond formation
    • Hoober, K. L., and Thorpe, C. (1999) Egg white sulfhydryl oxidase: Kinetic mechanism of the catalysis of disulfide bond formation. Biochemistry 38, 3211-3217.
    • (1999) Biochemistry , vol.38 , pp. 3211-3217
    • Hoober, K.L.1    Thorpe, C.2
  • 23
    • 10644295071 scopus 로고    scopus 로고
    • Flavoprotein disulfide reductases: Advances in chemistry and function
    • Argyrou, A., and Blanchard, J. S. (2004) Flavoprotein disulfide reductases: advances in chemistry and function. Prog. Nucleic Acid Res. Mol. Biol. 78, 89-142.
    • (2004) Prog. Nucleic Acid Res. Mol. Biol , vol.78 , pp. 89-142
    • Argyrou, A.1    Blanchard, J.S.2
  • 24
    • 0033527552 scopus 로고    scopus 로고
    • Homology between egg white sulfhydryl oxidase and quiescin Q6 defines a new class of flavin-linked sulfhydryl oxidases
    • Hoober, K. L., Glynn, N. M., Burnside, J., Coppock, D. L., and Thorpe, C. (1999) Homology between egg white sulfhydryl oxidase and quiescin Q6 defines a new class of flavin-linked sulfhydryl oxidases. J. Biol. Chem. 274, 31759-31762.
    • (1999) J. Biol. Chem , vol.274 , pp. 31759-31762
    • Hoober, K.L.1    Glynn, N.M.2    Burnside, J.3    Coppock, D.L.4    Thorpe, C.5
  • 25
    • 0035958044 scopus 로고    scopus 로고
    • Rat seminal vesicle FAD-dependent sulfhydryl oxidase: Biochemical characterization and molecular cloning of a member of the new sulfhydryl oxidase/quiescin Q6 gene family
    • Benayoun, B., Esnard-Fève, A., Castella, S., Courty, Y., and Esnard, F. (2001) Rat seminal vesicle FAD-dependent sulfhydryl oxidase: biochemical characterization and molecular cloning of a member of the new sulfhydryl oxidase/quiescin Q6 gene family. J. Biol. Chem. 276, 13830-13837.
    • (2001) J. Biol. Chem , vol.276 , pp. 13830-13837
    • Benayoun, B.1    Esnard-Fève, A.2    Castella, S.3    Courty, Y.4    Esnard, F.5
  • 27
    • 28444436253 scopus 로고    scopus 로고
    • Structural determinants of substrate access to the disulfide oxidase Erv2p
    • Vala, A., Sevier, C. S., and Kaiser, C. A. (2005) Structural determinants of substrate access to the disulfide oxidase Erv2p. J. Mol. Biol. 354, 952-966.
    • (2005) J. Mol. Biol , vol.354 , pp. 952-966
    • Vala, A.1    Sevier, C.S.2    Kaiser, C.A.3
  • 28
    • 0017166209 scopus 로고
    • Spectral evidence for a flavin adduct in a monoalkylated derivative of pig heart lipoamide dehydrogenase
    • Thorpe, C., and Williams, C. H. (1976) Spectral evidence for a flavin adduct in a monoalkylated derivative of pig heart lipoamide dehydrogenase. J. Biol. Chem. 251, 7726-7728.
    • (1976) J. Biol. Chem , vol.251 , pp. 7726-7728
    • Thorpe, C.1    Williams, C.H.2
  • 29
    • 0028108347 scopus 로고
    • Activation of molecular oxygen by flavins and flavoproteins
    • Massey, V. (1994) Activation of molecular oxygen by flavins and flavoproteins. J. Biol. Chem. 269, 22459-22462.
    • (1994) J. Biol. Chem , vol.269 , pp. 22459-22462
    • Massey, V.1
  • 30
    • 33646348711 scopus 로고    scopus 로고
    • To be or not to be an oxidase: Challenging the oxygen reactivity of flavoenzymes
    • Mattevi, A. (2006) To be or not to be an oxidase: challenging the oxygen reactivity of flavoenzymes. Trends Biochem. Sci. 31, 276-283.
    • (2006) Trends Biochem. Sci , vol.31 , pp. 276-283
    • Mattevi, A.1
  • 32
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet, F. (1988) Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16, 10881-10890.
    • (1988) Nucleic Acids Res , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 33
    • 30344444015 scopus 로고    scopus 로고
    • The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites
    • Tian, G., Xiang, S., Noiva, R., Lennarz, W. J., and Schindelin, H. (2006) The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites. Cell 124, 61-73.
    • (2006) Cell , vol.124 , pp. 61-73
    • Tian, G.1    Xiang, S.2    Noiva, R.3    Lennarz, W.J.4    Schindelin, H.5
  • 34
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede, T., Kopp, J., Guex, N., and Peitsch, M. C. (2003) SWISS-MODEL: An automated protein homology-modeling server. Nucleic Acids Res. 31, 3381-3385.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 36
    • 0032581420 scopus 로고    scopus 로고
    • The nonactive site cysteine residues of yeast protein disulfide isomerase are not required for cell viability
    • Luz, J. M., and Lennarz, W. J. (1998) The nonactive site cysteine residues of yeast protein disulfide isomerase are not required for cell viability. Biochem. Biophys. Res. Commun. 248, 621-627.
    • (1998) Biochem. Biophys. Res. Commun , vol.248 , pp. 621-627
    • Luz, J.M.1    Lennarz, W.J.2
  • 37
    • 9644279595 scopus 로고    scopus 로고
    • The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum
    • Xiao, R., Wilkinson, B., Solovyov, A., Winther, J. R., Holmgren, A., Lundstrom-Ljung, J., and Gilbert, H. F. (2004) The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum. J. Biol. Chem. 279, 49780-49786.
    • (2004) J. Biol. Chem , vol.279 , pp. 49780-49786
    • Xiao, R.1    Wilkinson, B.2    Solovyov, A.3    Winther, J.R.4    Holmgren, A.5    Lundstrom-Ljung, J.6    Gilbert, H.F.7
  • 38
    • 15744380512 scopus 로고    scopus 로고
    • A structural disulfide of yeast protein-disulfide isomerase destabilizes the active site disulfide of the N-terminal thioredoxin domain
    • Wilkinson, B., Xiao, R., and Gilbert, H. F. (2005) A structural disulfide of yeast protein-disulfide isomerase destabilizes the active site disulfide of the N-terminal thioredoxin domain. J. Biol. Chem. 280, 11483-11487.
    • (2005) J. Biol. Chem , vol.280 , pp. 11483-11487
    • Wilkinson, B.1    Xiao, R.2    Gilbert, H.F.3
  • 39
    • 0026738643 scopus 로고
    • The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase
    • Tachibana, C., and Stevens, T. H. (1992) The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol. Cell. Biol. 12, 4601-4611.
    • (1992) Mol. Cell. Biol , vol.12 , pp. 4601-4611
    • Tachibana, C.1    Stevens, T.H.2
  • 40
    • 0033230434 scopus 로고    scopus 로고
    • Eps1, a novel PDI-related protein involved in ER quality control in yeast
    • Wang, Q., and Chang, A. (1999) Eps1, a novel PDI-related protein involved in ER quality control in yeast. EMBO J. 18, 5972-5982.
    • (1999) EMBO J , vol.18 , pp. 5972-5982
    • Wang, Q.1    Chang, A.2
  • 41
    • 0029115691 scopus 로고
    • Isolation and characterization of a yeast gene, MPD1, the overexpression of which suppresses inviability caused by protein disulfide isomerase depletion
    • Tachikawa, H., Takeuchi, Y., Funahashi, W., Miura, T., Gao, X. D., Fujimoto, D., Mizunaga, T., and Onodera, K. (1995) Isolation and characterization of a yeast gene, MPD1, the overexpression of which suppresses inviability caused by protein disulfide isomerase depletion. FEBS Lett. 369, 212-216.
    • (1995) FEBS Lett , vol.369 , pp. 212-216
    • Tachikawa, H.1    Takeuchi, Y.2    Funahashi, W.3    Miura, T.4    Gao, X.D.5    Fujimoto, D.6    Mizunaga, T.7    Onodera, K.8
  • 43
    • 33947388374 scopus 로고    scopus 로고
    • Erv2p: Characterization of the redox behavior of a yeast sulfhydryl oxidase
    • Wang, W., Winther, J. R., and Thorpe, C. (2007) Erv2p: characterization of the redox behavior of a yeast sulfhydryl oxidase. Biochemistry 46, 3246-3254.
    • (2007) Biochemistry , vol.46 , pp. 3246-3254
    • Wang, W.1    Winther, J.R.2    Thorpe, C.3
  • 44
    • 0037395242 scopus 로고    scopus 로고
    • The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre
    • Hofhaus, G., Lee, J. E., Tews, I., Rosenberg, B., and Lisowsky, T. (2003) The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre. Eur. J. Biochem. 270, 1528-1535.
    • (2003) Eur. J. Biochem , vol.270 , pp. 1528-1535
    • Hofhaus, G.1    Lee, J.E.2    Tews, I.3    Rosenberg, B.4    Lisowsky, T.5
  • 45
    • 0017148370 scopus 로고
    • Interaction of phenols with old yellow enzyme. Physical evidence for charge-transfer complexes
    • Abramovitz, A. S., and Massey, V. (1976) Interaction of phenols with old yellow enzyme. Physical evidence for charge-transfer complexes. J. Biol. Chem. 251, 5327-5336.
    • (1976) J. Biol. Chem , vol.251 , pp. 5327-5336
    • Abramovitz, A.S.1    Massey, V.2
  • 46
    • 0001409925 scopus 로고
    • Role of charge-transfer interactions in flavoprotein catalysis
    • Massey, V., and Ghisla, S. (1974) Role of charge-transfer interactions in flavoprotein catalysis. Ann. N. Y. Acad. Sci. 227, 446-465.
    • (1974) Ann. N. Y. Acad. Sci , vol.227 , pp. 446-465
    • Massey, V.1    Ghisla, S.2
  • 47
    • 0017067595 scopus 로고
    • Differential reactivity of the two active site cysteine residues generated on reduction of pig heart lipoamide dehydrogenase
    • Thorpe, C., and Williams, C. H., Jr. (1976) Differential reactivity of the two active site cysteine residues generated on reduction of pig heart lipoamide dehydrogenase. J. Biol. Chem. 251, 3553-3557.
    • (1976) J. Biol. Chem , vol.251 , pp. 3553-3557
    • Thorpe, C.1    Williams Jr., C.H.2
  • 48
    • 0018786078 scopus 로고
    • Evidence for multiple electronic forms of two-electron-reduced lipoamide dehydrogenase from Escherichia coli
    • Wilkinson, K. D., and Williams, C. H., Jr. (1979) Evidence for multiple electronic forms of two-electron-reduced lipoamide dehydrogenase from Escherichia coli. J. Biol. Chem. 254, 852-862.
    • (1979) J. Biol. Chem , vol.254 , pp. 852-862
    • Wilkinson, K.D.1    Williams Jr., C.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.