Insights into the Mechanism of the Antibiotic‐Synthesizing Enzyme MoeO5 from Crystal Structures of Different Complexes | Zendy

Ren Feifei | Zendy; Ko TzuPing | Zendy; Feng Xinxin | Zendy; Huang ChunHsiang | Zendy; Chan HsiuChien | Zendy; Hu Yumei | Zendy; Wang Ke | Zendy; Ma Yanhe | Zendy; Liang PoHuang | Zendy; Wang Andrew H.J. | Zendy; Oldfield Eric | Zendy; Guo ReyTing | Zendy

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Insights into the Mechanism of the Antibiotic‐Synthesizing Enzyme MoeO5 from Crystal Structures of Different Complexes

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.201108002

Subject(s) - triosephosphate isomerase , stereochemistry , barrel (horology) , chemistry , moiety , isomerase , farnesyl pyrophosphate , pyrophosphate , crystallography , enzyme , ligand (biochemistry) , biochemistry , materials science , receptor , atp synthase , composite material

Barrel‐shaped : The enzyme MoeO5 catalyzes the transfer of the C 15 moiety of farnesyl pyrophosphate to the 2‐hydroxy group of 3‐phosphoglycerate to give 2‐( Z , E )‐farnesyl‐3‐phosphoglycerate (FPG; ligand in the center of the shown structure). X‐ray crystallographic structures showed that MoeO5 forms a triose‐phosphate‐isomerase barrel structure and binds FPG in a curved pocket, mainly as a result of its long λ3 loop (magenta in picture).

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