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Functional Analysis of the Aureothin Iterative Type I Polyketide Synthase
Author(s) -
He Jing,
Hertweck Christian
Publication year - 2005
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200400333
Subject(s) - polyketide synthase , polyketide , acyltransferase , computational biology , biosynthesis , atp synthase , biochemistry , chemistry , biology , stereochemistry , enzyme
The modular‐type polyketide synthase (PKS) that is involved in aureothin ( aur ) biosynthesis represents one of the first examples in which a single PKS module (AurA) is used in an iterative fashion. Here we report on the heterologous expression of an engineered AurAB fusion protein that unequivocally proves the iterative nature of AurA. In addition, point mutations reveal that aur PKS module 4 participates in polyketide biosynthesis despite its aberrant acyltransferase domain.