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Back Cover: Insights into the Mechanism of the Antibiotic‐Synthesizing Enzyme MoeO5 from Crystal Structures of Different Complexes (Angew. Chem. Int. Ed. 17/2012)
Author(s) -
Ren Feifei,
Ko TzuPing,
Feng Xinxin,
Huang ChunHsiang,
Chan HsiuChien,
Hu Yumei,
Wang Ke,
Ma Yanhe,
Liang PoHuang,
Wang Andrew H.J.,
Oldfield Eric,
Guo ReyTing
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201201339
Subject(s) - double bond , isomerase , triosephosphate isomerase , stereochemistry , int , enzyme , chemistry , prenyltransferase , antibiotics , barrel (horology) , multiple drug resistance , mechanism (biology) , staphylococcus aureus , transferase , biosynthesis , biochemistry , bacteria , biology , materials science , physics , genetics , organic chemistry , computer science , operating system , quantum mechanics , composite material
New antibiotics are needed because of the increasing occurrence of multidrug resistance, as seen in Staphylococcus aureus (MRSA). The initiating step of the biosynthesis of the next‐generation drug moenomycin is catalyzed by MoeO5, which is a prenyltransferase with triose‐phosphate‐isomerase barrel structure as was shown by E. Oldfield, R.‐T. Guo, and co‐workers in their Communication on page 4157 ff. The transferred farnesyl group undergoes a trans ‐to‐ cis conversion in its first double bond.