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

Content Provider	Royal Society of Chemistry (RSC)
Author	Villamizar, Germán Calle, Fernando de Garneau-Tsodikova, Sylvie Mady, Ahmed S. A. Zolova, Olga E. Millán, María Álvarez San Lombó, Felipe
Copyright Year	2011
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.
Starting Page	1999
Ending Page	2011
Page Count	13
File Format	HTM / HTML PDF
ISSN	1742206X
Volume Number	7
Issue Number	6
Journal	Molecular BioSystems
DOI	10.1039/c1mb05044c
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Gene Enzyme Micromonospora DNA Protein
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Biotechnology

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