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The structural biology of enzymes involved in natural product glycosylation

期刊

NATURAL PRODUCT REPORTS
卷 29, 期 10, 页码 1201-1237

出版社

ROYAL SOC CHEMISTRY
DOI: 10.1039/c2np20039b

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资金

  1. NIH [AI52218, CA84374, PSI GM098248]
  2. NATIONAL CANCER INSTITUTE [R01CA084374] Funding Source: NIH RePORTER
  3. NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R37AI052218, R01AI052218] Funding Source: NIH RePORTER
  4. NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [U01GM098248] Funding Source: NIH RePORTER

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The glycosylation of microbial natural products often dramatically influences the biological and/or pharmacological activities of the parental metabolite. Over the past decade, crystal structures of several enzymes involved in the biosynthesis and attachment of novel sugars found appended to natural products have emerged. In many cases, these studies have paved the way to a better understanding of the corresponding enzyme mechanism of action and have served as a starting point for engineering variant enzymes to facilitate to production of differentially-glycosylated natural products. This review specifically summarizes the structural studies of bacterial enzymes involved in biosynthesis of novel sugar nucleotides.

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