Crucial effect of the first CXXC motif of human QSOX 1b on the activity to different substrates

Journal of Biochemistry

Volumn 149, Issue 3, 2011, Pages 293-300

  Zheng, Wenyun ^a,b   Chu, Yanyan ^b   Yin, Qin ^a,b   Xu, Lei ^a,b   Yang, Charles ^a,b   Zhang, Wenyao ^a,b   Tang, Yun ^b   Yang, Yi ^a,b  

^a EAST CHINA UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

^b EAST CHINA UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

Author keywords

electron transfer; molecular modelling; QSOX; site directed mutagenesis; thiol oxidation

Indexed keywords

CYSTEINE; DISULFIDE; DITHIOTHREITOL; GLUTATHIONE; HOMOCYSTEINE; MERCAPTOETHANOL; PHOSPHINE; QUIESCIN SULPHHYDRYL OXIDASE 1B; THIOL OXIDASE; TRIS(2 CARBOXYETHYL)PHOSPHINE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ELECTRON TRANSPORT; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; MOLECULAR MODEL; NUCLEOTIDE SEQUENCE; OXIDATION; PROTEIN FUNCTION; PROTEIN MOTIF; SITE DIRECTED MUTAGENESIS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; CYTOCHROME REDUCTASES; DITHIOTHREITOL; ELECTRON TRANSPORT; HUMANS; MEMBRANE GLYCOPROTEINS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OXIDOREDUCTASES; OXIDOREDUCTASES ACTING ON SULFUR GROUP DONORS; PEROXIDASES; PHOSPHINES;

EID: 79952285027     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvq143     Document Type: Article

References (33)

1. Ostrowski, M.C. and Kistler, W.S. (1980) Properties of a flavoprotein sulfhydryl oxidase from rat seminal vesicle secretion. Biochemistry 19, 2639-2645
2. Brohawn, S.G., Miksa, I.R., and Thorpe, C. (2003) Avian sulfhydryl oxidase is not a metalloenzyme: adventitious binding of divalent metal ions to the enzyme. Biochemistry 42, 11074-11082 (Pubitemid 37174400)
3. 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 (Pubitemid 36457625)
4. Hoober, K.L., Joneja, B., White, H.B. 3rd, and Thorpe, C. (1996) A sulfhydryl oxidase from chicken egg white. J. Biol. Chem. 271, 30510-30516
5. Hoober, K.L., Sheasley, S.L., 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
6. Hoober, K.L. and Thorpe, C. (1999) Egg white sulfhydryl oxidase: kinetic mechanism of the catalysis of disulfide bond formation. Biochemistry 38, 3211-3217
7. 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
8. 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 (Pubitemid 36505444)
9. 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
10. Heckler, E.J., Alon, A., Fass, D., and Thorpe, C. (2008) Human quiescin-sulfhydryl oxidase, QSOX1: probing internal redox steps by mutagenesis. Biochemistry 47, 4955-4963
11. Raje, S., Glynn, N.M., and Thorpe, C. (2002) A continuous fluorescence assay for sulfhydryl oxidase. Anal. Biochem. 307, 266-272
12. UniprotKB. http://www.uniprot.org/
13. Marsden, R.L., McGuffin, L.J., and Jones, D.T. (2002) Rapid protein domain assignment from amino acid sequence using predicted secondary structure. Protein Sci. 11, 2814-2824 (Pubitemid 35365248)
14. Sali, A. and Blundell, T.L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815
15. 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 (Pubitemid 43069310)
16. Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F., and Higgins, D.G. (1997) The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25, 4876-4882 (Pubitemid 28022245)
17. Laskowski, R., Macarthur, M., Moss, D., and Thornton, J. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291
18. Alon, A., Heckler, E.J., Thorpe, C., and Fass, D. (2010) QSOX contains a pseudo-dimer of functional and degenerate sulfhydryl oxidase domains. FEBS Lett. 584, 1521-1525
19. Dominguez, C., Boelens, R., and Bonvin, A.M. (2003) HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. J. Am. Chem. Soc. 125, 1731-1737
20. de Vries, S.J., van Dijk, A.D., Krzeminski, M., van Dijk, M., Thureau, A., Hsu, V., Wassenaar, T., and Bonvin, A.M. (2007) HADDOCK versus HADDOCK: new features and performance of HADDOCK2.0 on the CAPRI targets. Proteins 69, 726-733 (Pubitemid 350210131)
21. Schneidman-Duhovny, D., Inbar, Y., Nussinov, R., and Wolfson, H.J. (2005) PatchDock and SymmDock: servers for rigid and symmetric docking. Nucleic Acids Res. 33, W363-W367 (Pubitemid 44529944)
22. Duhovny, D., Nussinov, R., and Wolfson, H.J. (2002) Efficient Unbound Docking of Rigid Molecules. Proceedings of the 2'nd Workshop on Algorithms in Bioinformatics (WABI), Rome, Italy, Lecture Notes in Computer Science 2452 (Gusfield et al., eds.), pp. 185-200, Springer Verlag
23. MacroModel, version 9.6, Schrödinger, LLC, New York, NY, 2008
24. SiteMap, version 2.2, Schrödinger, LLC, New York, NY, 2008
25. Glide, version 5.0, Schrödinger, LLC, New York, NY, 2008
26. Lee, J., Hofhaus, G., and Lisowsky, T. (2000) Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase. FEBS Lett. 477, 62-66 (Pubitemid 30438858)
27. 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
28. Stein, G. and Lisowsky, T. (1998) Functional comparison of the yeast scERV1 and scERV2 genes. Yeast 14, 171-180 (Pubitemid 28062867)
29. 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
30. Benayoun, B., Esnard-Feve, 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
31. Coppock, D.L., Cina-Poppe, D., and Gilleran, S. (1998) The quiescin Q6 gene (QSCN6) is a fusion of two ancient gene families: thioredoxin and ERV1. Genomics 54, 460-468 (Pubitemid 29036233)
32. Herrmann, J.M., Kauff, F., and Neuhaus, H.E. (2009) Thiol oxidation in bacteria, mitochondria and chloroplasts: common principles but three unrelated machineries? Biochim. Biophys. Acta 1793, 71-77
33. Thorpe, C., Hoober, K.L., Raje, S., Glynn, N.M., Burnside, J., Turi, G.K., and Coppock, D.L. (2002) Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes. Arch. Biochem. Biophys. 405, 1-12