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Functionally Distinct Modules Operate Two Consecutive α,β→β,γ Double‐Bond Shifts in the Rhizoxin Polyketide Assembly Line
Author(s) -
Kusebauch Björn,
Busch Benjamin,
Scherlach Kirstin,
Roth Martin,
Hertweck Christian
Publication year - 2010
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.200905467
Subject(s) - moiety , domain (mathematical analysis) , stereochemistry , chemistry , computer science , mathematics , mathematical analysis
Shift work : Biochemical analysis of the rhizoxin pathway revealed that the diene moiety is not shifted all at once, but through distinct enzymatic operations. The first shift occurs by a formal β,γ‐dehydration in module 7, while the second double bond is first generated by module 8 and then shifted by an unprecedented “shift module” with a novel type of DH* domain (see scheme). ACP=acyl carrier protein, DH*=dehydratase‐like shift domain.