Enzymatic Timing and Tailoring of Macrolactamization in Syringolin Biosynthesis

Enzymatic Timing and Tailoring of Macrolactamization in Syringolin Biosynthesis

The enzymatic activation of 3,4-dehydrolysine and subsequent formation of the 12-membered syringolin macrolactam were investigated. The timing of the desaturation was elucidated through the analysis of the initial adenylation domain of SylD. The SylD-TTE didomain was characterized and demonstrated t...

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Veröffentlicht in:Organic letters 2011-09, Vol.13 (17), p.4518-4521
Hauptverfasser: Wuest, William M, Krahn, Daniel, Kaiser, Markus, Walsh, Christopher T
Format: Artikel
Sprache:eng
Schlagworte:
Molecular Structure
Peptides, Cyclic - biosynthesis
Peptides, Cyclic - chemistry
Stereoisomerism
Thiolester Hydrolases - chemistry
Thiolester Hydrolases - metabolism
Urea - analogs & derivatives
Urea - chemistry
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Zusammenfassung:The enzymatic activation of 3,4-dehydrolysine and subsequent formation of the 12-membered syringolin macrolactam were investigated. The timing of the desaturation was elucidated through the analysis of the initial adenylation domain of SylD. The SylD-TTE didomain was characterized and demonstrated to be the catalyst for formation of 12-membered macrocycles. When the SylD thioesterase domain was reacted with a family of acyclic CoA both natural and unnatural macrocycles were generated.
ISSN:1523-7060
1523-7052
DOI:10.1021/ol2016687