期刊
CHEMISTRY & BIOLOGY
卷 18, 期 4, 页码 542-552出版社
CELL PRESS
DOI: 10.1016/j.chembiol.2010.12.022
关键词
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资金
- Science Foundation Ireland [RFP/GEN/F571]
- PRTLI
- Marie Curie Fellowship
- UK BBSRC [BB/H006281/1]
- Higher Education Authority
- Health Research Board
- BBSRC [BB/H006281/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/H006281/1] Funding Source: researchfish
Gliotoxin, a redox-active metabolite, is produced by the opportunistic fungal pathogen Aspergillus fumigatus, and its biosynthesis is directed by the gli gene cluster. Knowledge of the biosynthetic pathway to gliotoxin, which contains a disulfide bridge of unknown origin, is limited, although L-Phe and L-Ser are known biosynthetic precursors. Deletion of gliG from the gli cluster, herein functionally confirmed as a glutathione S-transferase, results in abrogation of gliotoxin biosynthesis and accumulation of 6-benzy1-6-hydroxy-1-methoxy-3-methylene-piperazine-2,5-dione. This putative shunt metabolite from the gliotoxin biosynthetic pathway contains an intriguing hydroxyl group at C-6, consistent with a gliotoxin biosynthetic pathway involving thiolation via addition of the glutathione thiol group to a reactive acyl imine intermediate. Complementation of gliG restored gliotoxin production and, unlike gliT, gliG was found not to be involved in fungal self-protection against gliotoxin.
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