Flavoenzyme-catalyzed formation of disulfide bonds in natural products

Angewandte Chemie - International Edition

Volumn 53, Issue 8, 2014, Pages 2221-2224

  Scharf, Daniel H ^b   Groll, Michael ^a   Habel, Andreas ^b   Heinekamp, Thorsten ^b   Hertweck, Christian ^b   Brakhage, Axel A ^b   Huber, Eva M ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

Author keywords

disulfide bonds; enzyme catalysis; natural products; oxidoreductases; sulfur

Indexed keywords

DISULFIDE BONDS; ENZYME CATALYSIS; MUTAGENESIS EXPERIMENT; NATURAL PRODUCTS; OXIDO-REDUCTASES; REACTION MECHANISM; SUBSTRATE BINDING; VIRULENCE FACTORS;

BIOACTIVITY; CATALYSIS; COVALENT BONDS; SULFUR; X RAY CRYSTALLOGRAPHY;

ENZYMES;

BACTERIAL PROTEIN; BIOLOGICAL PRODUCT; DEPSIPEPTIDE; DISULFIDE; FUNGAL PROTEIN; GLIOTOXIN; HOLOMYCIN; LACTAM; OXIDOREDUCTASE; ROMIDEPSIN;

ASPERGILLUS FUMIGATUS; BINDING SITE; BIOCATALYSIS; CHEMISTRY; CHROMOBACTERIUM; ENZYME SPECIFICITY; ENZYMOLOGY; METABOLISM; OXIDATION REDUCTION REACTION; PROTEIN TERTIARY STRUCTURE; STREPTOMYCES; X RAY CRYSTALLOGRAPHY;

ASPERGILLUS FUMIGATUS; BACTERIAL PROTEINS; BINDING SITES; BIOCATALYSIS; BIOLOGICAL PRODUCTS; CHROMOBACTERIUM; CRYSTALLOGRAPHY, X-RAY; DEPSIPEPTIDES; DISULFIDES; FUNGAL PROTEINS; GLIOTOXIN; LACTAMS; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEIN STRUCTURE, TERTIARY; STREPTOMYCES; SUBSTRATE SPECIFICITY;

EID: 84893851464     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201309302     Document Type: Article

References (23)

1. T. R. Dagenais, N. P. Keller, Clin. Microbiol. Rev. 2009, 22, 447-465.
2. K. J. Kwon-Chung, J. A. Sugui, Med. Mycol. 2009, 47, Suppl. 1, S 97-103.
3. D. M. Gardiner, P. Waring, B. J. Howlett, Microbiology 2005, 151, 1021-1032.
4. D. H. Scharf, T. Heinekamp, N. Remme, P. Hortschansky, A. A. Brakhage, C. Hertweck, Appl. Microbiol. Biotechnol. 2012, 93, 467-472.
5. C. J. Balibar, C. T. Walsh, Biochemistry 2006, 45, 15029-15038
6. R. A. Cramer, Jr., M. P. Gamcsik, R. M. Brooking, L. K. Najvar, W. R. Kirkpatrick, T. F. Patterson, C. J. Balibar, J. R. Graybill, J. R. Perfect, S. N. Abraham, W. J. Steinbach, Eukaryotic Cell 2006, 5, 972-980.
7. D. H. Scharf, N. Remme, A. Habel, P. Chankhamjon, K. Scherlach, T. Heinekamp, P. Hortschansky, A. A. Brakhage, C. Hertweck, J. Am. Chem. Soc. 2011, 133, 12322-12325.
8. D. H. Scharf, P. Chankhamjon, K. Scherlach, T. Heinekamp, M. Roth, A. A. Brakhage, C. Hertweck, Angew. Chem. 2012, 124, 10211-10215
9. Angew. Chem. Int. Ed. 2012, 51, 10064-10068
10. D. H. Scharf, P. Chankhamjon, K. Scherlach, T. Heinekamp, K. Willing, A. A. Brakhage, C. Hertweck, Angew. Chem. 2013, 125, 11298-11301
11. Angew. Chem. Int. Ed. 2013, 52, 11092-11095.
12. D. H. Scharf, N. Remme, T. Heinekamp, P. Hortschansky, A. A. Brakhage, C. Hertweck, J. Am. Chem. Soc. 2010, 132, 10136-10141
13. M. Schrettl, S. Carberry, K. Kavanagh, H. Haas, G. W. Jones, J. O'Brien, A. Nolan, J. Stephens, O. Fenelon, S. Doyle, PLoS Pathog. 2010, 6, e 1000952.
14. B. Li, C. T. Walsh, Biochemistry 2011, 50, 4615-4622
15. C. Wang, S. R. Wesener, H. Zhang, Y. Q. Cheng, Chem. Biol. 2009, 16, 585-593.
16. D. Mustacich, G. Powis, Biochem. J. 2000, 346 Pt 1, 1-8.
17. G. Waksman, T. S. Krishna, C. H. Williams, Jr., J. Kuriyan, J. Mol. Biol. 1994, 236, 800-816.
18. P. A. Karplus, G. E. Schulz, J. Mol. Biol. 1987, 195, 701-729.
19. C. Thorpe, C. H. Williams, Jr., J. Biol. Chem. 1976, 251, 3553-3557.
20. E. J. Heckler, P. C. Rancy, V. K. Kodali, C. Thorpe, Biochim. Biophys. Acta Mol. Cell Res. 2008, 1783, 567-577
21. C. Thorpe, K. L. Hoober, S. Raje, N. M. Glynn, J. Burnside, G. K. Turi, D. L. Coppock, Arch. Biochem. Biophys. 2002, 405, 1-12.
22. A. Mattevi, A. J. Schierbeek, W. G. Hol, J. Mol. Biol. 1991, 220, 975-994.
23. B. W. Lennon, C. H. Williams, Jr., M. L. Ludwig, Science 2000, 289, 1190-1194.