Characterization of TioQ, a type II thioesterase from the thiocoraline biosynthetic cluster

Ahmed S.A. Mady, Olga E. Zolova, María Álvarez San Millán, Germán Villamizar, Fernando De La Calle, Felipe Lombó, Sylvie Garneau-Tsodikova

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

An antitumor agent thiocoraline is a thiodepsipeptide marine product derived from two Micromonospora sp. strains that inhibits protein synthesis by binding of its key 3-hydroxyquinaldic acid (3HQA) chromophores to duplex DNA. There are at least two potential pathways via which the 3HQA moiety could be biosynthesized from l-Trp. By biochemical characterization and by preparation of knockouts of an adenylation-thiolation enzyme, TioK, and of two type II thioesterases, TioP and TioQ, found in the thiocoraline biosynthetic gene cluster, we gained valuable insight into the pathway followed for the production of 3HQA.

Original languageEnglish
Pages (from-to)1999-2011
Number of pages13
JournalMolecular BioSystems
Volume7
Issue number6
DOIs
StatePublished - Jun 1 2011

ASJC Scopus subject areas

  • Biotechnology
  • Molecular Biology

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