Post-Polyketide Synthase Steps in Iso-migrastatin Biosynthesis, Featuring Tailoring Enzymes with Broad Substrate Specificity

Post-Polyketide Synthase Steps in Iso-migrastatin Biosynthesis, Featuring Tailoring Enzymes with Broad Substrate Specificity

The iso-migrastatin (iso-MGS) bio­synthetic gene cluster from Strepto­myces platensis NRRL 18993 consists of 11 genes, featuring an acyl­transferase (AT)-less type I poly­ketide synthase (PKS) and three tailoring enzymes MgsIJK. Systematic inactivation of mgsIJK in S. platensis enabled us to (i) ide...

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Veröffentlicht in:Journal of the American Chemical Society 2013-02, Vol.135 (7), p.2489-2492
Hauptverfasser: Ma, Ming, Kwong, Thomas, Lim, Si-Kyu, Ju, Jianhua, Lohman, Jeremy R, Shen, Ben
Format: Artikel
Sprache:eng
Schlagworte:
Biosynthetic Pathways
Macrolides - chemistry
Molecular Structure
Piperidones - chemistry
Polyketide Synthases - chemistry
Streptomyces - enzymology
Streptomyces - genetics
Substrate Specificity
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Zusammenfassung:The iso-migrastatin (iso-MGS) bio­synthetic gene cluster from Strepto­myces platensis NRRL 18993 consists of 11 genes, featuring an acyl­transferase (AT)-less type I poly­ketide synthase (PKS) and three tailoring enzymes MgsIJK. Systematic inactivation of mgsIJK in S. platensis enabled us to (i) identify two nascent products of the iso-MGS AT-less type I PKS, establishing an unprecedented novel feature for AT-less type I PKSs, and (ii) account for the formation of all known post-PKS bio­synthetic intermediates generated by the three tailoring enzymes MgsIJK, which possessed significant substrate promiscuities.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja4002635