Please use this identifier to cite or link to this item:
https://doi.org/10.1002/anie.201307404
DC Field | Value | |
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dc.title | Conversion of a disulfide bond into a thioacetal group during echinomycin biosynthesis | |
dc.contributor.author | Hotta, K. | |
dc.contributor.author | Keegan, R.M. | |
dc.contributor.author | Ranganathan, S. | |
dc.contributor.author | Fang, M. | |
dc.contributor.author | Bibby, J. | |
dc.contributor.author | Winn, M.D. | |
dc.contributor.author | Sato, M. | |
dc.contributor.author | Lian, M. | |
dc.contributor.author | Watanabe, K. | |
dc.contributor.author | Rigden, D.J. | |
dc.contributor.author | Kim, C.-Y. | |
dc.date.accessioned | 2014-10-27T08:24:42Z | |
dc.date.available | 2014-10-27T08:24:42Z | |
dc.date.issued | 2014 | |
dc.identifier.citation | Hotta, K., Keegan, R.M., Ranganathan, S., Fang, M., Bibby, J., Winn, M.D., Sato, M., Lian, M., Watanabe, K., Rigden, D.J., Kim, C.-Y. (2014). Conversion of a disulfide bond into a thioacetal group during echinomycin biosynthesis. Angewandte Chemie - International Edition 53 (3) : 824-828. ScholarBank@NUS Repository. https://doi.org/10.1002/anie.201307404 | |
dc.identifier.issn | 14337851 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/100338 | |
dc.description.abstract | Echinomycin is a nonribosomal depsipeptide natural product with a range of interesting bioactivities that make it an important target for drug discovery and development. It contains a thioacetal bridge, a unique chemical motif derived from the disulfide bond of its precursor antibiotic triostin A by the action of an S-adenosyl-L-methionine-dependent methyltransferase, Ecm18. The crystal structure of Ecm18 in complex with its reaction products S-adenosyl-L-homocysteine and echinomycin was determined at 1.50 Å resolution. Phasing was achieved using a new molecular replacement package called AMPLE, which automatically derives search models from structure predictions based on ab initio protein modelling. Structural analysis indicates that a combination of proximity effects, medium effects, and catalysis by strain drives the unique transformation of the disulfide bond into the thioacetal linkage. Disulfide to thioacetal: The S-adenosyl-L-methionine (SAM)-dependent methyltransferase Ecm 18 converts the disulfide bond of triostin A into a thioacetal linkage to form echinomycin. The 1.50 Å crystal structure of Ecm 18 in complex with its reaction products S-adenosyl-L-homocysteine (SAH) and echinomycin provides insight into how Ecm 18 catalyzes this unusual transformation. Copyright © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. | |
dc.description.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1002/anie.201307404 | |
dc.source | Scopus | |
dc.subject | biosynthesis | |
dc.subject | disulfides | |
dc.subject | peptides | |
dc.subject | thioacetals | |
dc.subject | transferases | |
dc.type | Article | |
dc.contributor.department | BIOLOGICAL SCIENCES | |
dc.description.doi | 10.1002/anie.201307404 | |
dc.description.sourcetitle | Angewandte Chemie - International Edition | |
dc.description.volume | 53 | |
dc.description.issue | 3 | |
dc.description.page | 824-828 | |
dc.description.coden | ACIEF | |
dc.identifier.isiut | 000330983300033 | |
Appears in Collections: | Staff Publications |
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