Review Article | Published:

Review Article

Biosynthesis of the Tunicamycins: A Review

The Journal of Antibiotics volume 60, pages 485491 (2007) | Download Citation

Subjects

Abstract

Tunicamycins are nucleotide sugar analogs produced by several Streptomyces species. In eukaryotes, tunicamycins inhibit UDP-N-acetylglucosamine: dolichol phosphate GlcNAc-1-P transferase (GPT) that catalyzes the first step in protein glycosylation. In bacteria they inhibit UDP-N-acetylmuramoyl-pentapeptide: undecaprenol phosphate MurNAc-pentapeptide-1-P transtransferase (MraY) that catalyzes an early stage in peptidoglycan cell wall assembly. Tunicamycins are substrate analog of GPT and MraY, such that the αβ-1″,11′-linked GlcNAc residue of the tunicamycins mimics the transferred GlcNAc-1-phosphate. The unusual structure of tunicamycins, particularly the unique 11-carbon sugar, tunicamine, and the αβ-1″,11′-O-glycosidic linkage, suggest its biosynthesis to be unique. This review discusses potential biosyntheses for tunicamycins via the synthesis and conjugation of uridine-5′-aldehyde and UDP-4-keto-N-acetylgalactosamine-5,6-ene and the subsequent formation of the α,β-1″,11′ glycosidic linkage.

Author information

Author notes

    • Billyana Tsvetanova

    Present address: Invitrogen Corporation, 1610 Faraday Avenue, Carlsbad, CA 92008

Affiliations

  1. USDA-ARS-NCAUR, Bioproducts and Biocatalysis Research Unit, 1815 North University Street, Peoria, IL 61604, U.S.A.

    • Neil P J Price
  2. The Scripps Research Institute (TSRI), 10550 North Torrey Pines Rd., MEM-116, La Jolla, CA 92037, U.S.A.

    • Billyana Tsvetanova

Authors

  1. Search for Neil P J Price in:

  2. Search for Billyana Tsvetanova in:

Corresponding author

Correspondence to Neil P J Price.

About this article

Publication history

Received

Accepted

Published

DOI

https://doi.org/10.1038/ja.2007.62

Further reading