Schneider_2008_Fungal.Genet.Biol_45_1487

Reference

Title : Characterization of the atromentin biosynthesis genes and enzymes in the homobasidiomycete Tapinella panuoides - Schneider_2008_Fungal.Genet.Biol_45_1487
Author(s) : Schneider P , Bouhired S , Hoffmeister D
Ref : Fungal Genet Biol , 45 :1487 , 2008
Abstract :

This report highlights the first biochemical characterization of a multi-domain biosynthetic enzyme for basidiomycete secondary metabolism: the tri-domain enzyme atromentin synthetase AtrA, from Tapinella panuoides, which adenylates and dimerizes 4-hydroxyphenylpyruvic acid into atromentin. Also, the l-tyrosine:2-oxoglutarate aminotransferase AtrD, which provides the substrate for this dimerization step, has been characterized. AtrA and AtrD expand the shikimic acid pathway from l-tyrosine to atromentin, the central terphenylquinone intermediate for a prominent and widely occurring class of basidiomycete pigments, among them various pharmaceutically relevant compounds. The genes atrA and atrD were cloned and found to be clustered within one genetic locus. Given the broad distribution of atromentin-derived compounds among homobasidiomycetes we expect our system represents a widely applicable model.

PubMedSearch : Schneider_2008_Fungal.Genet.Biol_45_1487
PubMedID: 18805498
Gene_locus related to this paper: tappa-atra

Related information

Gene_locus tappa-atra

Citations formats

Schneider P, Bouhired S, Hoffmeister D (2008)
Characterization of the atromentin biosynthesis genes and enzymes in the homobasidiomycete Tapinella panuoides
Fungal Genet Biol 45 :1487

Schneider P, Bouhired S, Hoffmeister D (2008)
Fungal Genet Biol 45 :1487