In:
Angewandte Chemie International Edition, Wiley, Vol. 53, No. 8 ( 2014-02-17), p. 2221-2224
Abstract:
Nature provides a rich source of compounds with diverse chemical structures and biological activities, among them, sulfur‐containing metabolites from bacteria and fungi. Some of these compounds bear a disulfide moiety that is indispensable for their bioactivity. Specialized oxidoreductases such as GliT, HlmI, and DepH catalyze the formation of this disulfide bridge in the virulence factor gliotoxin, the antibiotic holomycin, and the anticancer drug romidepsin, respectively. We have examined all three enzymes by X‐ray crystallography and activity assays. Despite their differently sized substrate binding clefts and hence, their diverse substrate preferences, a unifying reaction mechanism is proposed based on the obtained crystal structures and further supported by mutagenesis experiments.
Type of Medium:
Online Resource
ISSN:
1433-7851
,
1521-3773
DOI:
10.1002/anie.201309302
Language:
English
Publisher:
Wiley
Publication Date:
2014
detail.hit.zdb_id:
2011836-3
detail.hit.zdb_id:
123227-7
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