Vagstad_2012_Chem.Biol_19_1525

Reference

Title : Characterization of a fungal thioesterase having Claisen cyclase and deacetylase activities in melanin biosynthesis - Vagstad_2012_Chem.Biol_19_1525
Author(s) : Vagstad AL , Hill EA , Labonte JW , Townsend CA
Ref : Chemical Biology , 19 :1525 , 2012
Abstract :

Melanins are a broad class of darkly pigmented macromolecules formed by oxidative polymerization of phenolic monomers. In fungi, melanins are known virulence factors that contribute to pathogenicity. Their biosynthesis generally involves polymerization of 1,8-dihydroxynaphthalene via a 1,3,6,8-tetrahydroxynaphthalene (THN) precursor assembled by multidomain, nonreducing polyketide synthases. Convergent routes to THN have evolved in fungi. Parallel heptaketide and hexaketide pathways exist that utilize conventional C-terminal thioesterase/Claisen cyclase domains and separate side-chain deacylases. Here, in vitro characterization of Pks1 from Colletotrichum lagenarium establishes a true THN synthase with a bifunctional thioesterase (TE) catalyzing both cyclization and deacetylation of an enzyme-bound hexaketide substrate. Chimeric TE domains were generated by swapping lid regions of active sites between classes of melanin TEs to gain insight into this unprecedented catalysis of carbon-carbon bond making and breaking by an alpha/beta-hydrolase fold enzyme.

PubMedSearch : Vagstad_2012_Chem.Biol_19_1525
PubMedID: 23261597
Gene_locus related to this paper: glola-PKS1

Related information

Gene_locus glola-PKS1

Citations formats

Vagstad AL, Hill EA, Labonte JW, Townsend CA (2012)
Characterization of a fungal thioesterase having Claisen cyclase and deacetylase activities in melanin biosynthesis
Chemical Biology 19 :1525

Vagstad AL, Hill EA, Labonte JW, Townsend CA (2012)
Chemical Biology 19 :1525