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• W2558644420 endingPage "323" @default.
• W2558644420 startingPage "316" @default.
• W2558644420 abstract "Type II polyketide synthases iteratively generate a nascent polyketide thioester of the acyl carrier protein (ACP); this is structurally modified to produce an ACP-free intermediate towards the final metabolite. However, the timing of ACP off-loading is not well defined because of the lack of an apparent thioesterase (TE) among relevant biosynthetic enzymes. Here, ActIV, which had been assigned as a second ring cyclase (CYC) in actinorhodin (ACT) biosynthesis, was shown to possess TE activity in vitro with a model substrate, anthraquinone-2-carboxylic acid-N-acetylcysteamine. In order to investigate its function further, the ACT biosynthetic pathway in Streptomyces coelicolor A3(2) was reconstituted in vitro in a stepwise fashion up to (S)-DNPA, and the product of ActIV reaction was characterized as an ACP-free bicyclic intermediate. These findings indicate that ActIV is a bifunctional CYC-TE and provide clear evidence for the release timing of the intermediate from the ACP anchor." @default.
• W2558644420 created "2016-12-08" @default.
• W2558644420 creator A5001494964 @default.
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• W2558644420 creator A5049960679 @default.
• W2558644420 creator A5051226332 @default.
• W2558644420 creator A5084790628 @default.
• W2558644420 date "2017-01-12" @default.
• W2558644420 modified "2023-10-18" @default.
• W2558644420 title "Bifunctionality of ActIV as a Cyclase-Thioesterase Revealed by in Vitro Reconstitution of Actinorhodin Biosynthesis in<i>Streptomyces coelicolor</i>A3(2)" @default.
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• W2558644420 doi "https://doi.org/10.1002/cbic.201600589" @default.
• W2558644420 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27897367" @default.
• W2558644420 hasPublicationYear "2017" @default.
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