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B6db references: 18805498

type Journal Article
authors Schneider P, Bouhired S, Hoffmeister D.
title Characterization of the atromentin biosynthesis genes and enzymes in the homobasidiomycete Tapinella panuoides
journal Fungal Genet Biol
Activity 2.6.1.5
Family 2.6.1.5.b
sel selected
ui 18805498
year (2008)
volume 45
number 11
pages 1487-96
 
keywords DOI: 10.1016/j.fgb.2008.08.009
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.
last changed 2019/05/13 10:19

B6db references