High-throughput identification of catalytic redox-active cystein residues

Science

Volumn 315, Issue 5810, 2007, Pages 387-389

  Fomenko, Dmitri E ^a   Xing, Weibing ^b   Adair, Blakely M ^c   Thomas, David J ^c   Gladyshev, Vadim N ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

^b UNIVERSITY OF NORTH CAROLINA   (United States)

^c U S ENVIRONMENTAL PROTECTION AGENCY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; GLUTAREDOXIN; METHYLTRANSFERASE; OXIDOREDUCTASE; PEROXIDASE; PEROXIREDOXIN; PROTEIN; SELENOCYSTEINE; SELENOPROTEIN; SULFENIC ACID DERIVATIVE; THIOREDOXIN;

AMINO ACID; CATALYSIS; DATABASE; DETECTION METHOD; GENOMICS; IDENTIFICATION METHOD; PROTEIN; REDOX CONDITIONS;

ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; OPEN READING FRAME; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; ARCHAEAL PROTEINS; BACTERIAL PROTEINS; BASE SEQUENCE; CATALYSIS; COMPUTATIONAL BIOLOGY; CYSTEINE; DATABASES, NUCLEIC ACID; DATABASES, PROTEIN; ENZYMES; EUKARYOTIC CELLS; EVOLUTION, MOLECULAR; METHYLTRANSFERASES; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEINS; SELENOCYSTEINE; SELENOPROTEINS;

EID: 33846635882     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1133114     Document Type: Article

References (24)

1. M. Beeby et al., PLoS Biol. 3, e309 (2005).
2. D. E. Fomenko, V. N. Gladyshev, Biochemistry 42, 11214 (2003).
3. J. S. Fetrow et al., Protein Sci. 10, 1005 (2001).
4. L. I. Leichert, U. Jakob, PLoS Biol. 2, e333 (2004).
5. G. V. Kryukov et al., Science 300, 1439 (2003).
6. D. L. Hatfield, M. J. Berry, V. N. Gladyshev, Selenium: Its Molecular Biology and Role in Human Health (Springer, New York, 2006).
7. R. M. Tujebajeva et al., EMBO Rep. 1, 158 (2000).
8. P. R. Copeland, V. A. Stepanik, D. M. Driscoll, Mol. Cell. Biol. 21, 1491 (2001).
9. S. V. Novoselov et al., EMBO J. 21, 3681 (2002).
10. H. Y. Kim, V. N. Gladyshev, PLoS Biol. 3, e375 (2005).
11. S. F. Altschul et al., Nucleic Acids Res. 25, 3389 (1997).
12. Single-letter abbreviations for amino acid residues: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; Y, Tyr.
13. B. P. Rosen, FEBS Lett. 529, 86 (2002).
14. B. M. Adair et al., Environ. Chem. 2, 161 (2005).
15. S. B. Waters, M. Styblo, D. J. Thomas, Chem. Res. Toxicol. 17, 404 (2004).
16. J. Li et al., Toxicol. Appl. Pharmacol. 204, 164 (2005).
17. J. R. Cupp-Vickery, J. J. Silberg, D. T. Ta, L. E. Vickery, J. Mol. Biol. 338, 127 (2004).
18. C. Dahl et al., J. Bacteriol. 187, 1392 (2005).
19. J. D. Hayes, J. U. Flanagan, I. R. Jowsey, Annu. Rev. Pharmacol. Toxicol. 45, 51 (2005).
20. D. Bordo, P. Bork, EMBO Rep. 3, 741 (2002).
21. S. Leimkuhler, M. M. Wuebbens, K. V. Rajagopalan, J. Biol. Chem. 276, 34695 (2001).
22. S. Madadi-Kahkesh et al., Eur. J. Biochem. 268, 2566 (2001).
23. S. G. Tringe et al., Science 308, 554 (2005).
24. Supported by NIH grants GM061603 and AG021518 (V.N.G.) and by U.S. Environmental Protection Agency-University of North Carolina Toxicology Research Program training grant T901915 (W.X.).