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Glycosyltransferases from oat (Avena) implicated in the acylation of avenacins

ABSTRACT: To study glycosyltransferases from oat, root proteins were extracted and separated gy 1D SDS gel electrophoresis. Bands were cut out, digested with trypsin, and the resulting peptides were analysed by LCMSMS on an Orbitrap mass sepctrometer. Raw data was processed with MaxQuant 1.3.0.5, and database searches on a custom database performed using Mascot.

INSTRUMENT(S): LTQ Orbitrap, instrument model

ORGANISM(S): Avena Strigosa (black Oat)

SUBMITTER: Gerhard Saalbach

PROVIDER: PXD000083 | Pride | 2013-04-24

REPOSITORIES: Pride

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Glycosyltransferases from oat (Avena) implicated in the acylation of avenacins.

Owatworakit Amorn A Townsend Belinda B Louveau Thomas T Jenner Helen H Rejzek Martin M Hughes Richard K RK Saalbach Gerhard G Qi Xiaoquan X Bakht Saleha S Roy Abhijeet Deb AD Mugford Sam T ST Goss Rebecca J M RJ Field Robert A RA Osbourn Anne A

The Journal of biological chemistry 20121220 6

Plants produce a huge array of specialized metabolites that have important functions in defense against biotic and abiotic stresses. Many of these compounds are glycosylated by family 1 glycosyltransferases (GTs). Oats (Avena spp.) make root-derived antimicrobial triterpenes (avenacins) that provide protection against soil-borne diseases. The ability to synthesize avenacins has evolved since the divergence of oats from other cereals and grasses. The major avenacin, A-1, is acylated with N-methyl ...[more]

PMID: 23258535

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