Title : The Arabidopsis DUF231 domain-containing protein ESK1 mediates 2-O- and 3-O-acetylation of xylosyl residues in xylan.

Pub. Date : 2013 Jul

PMID : 23659919






2 Functional Relationships(s)
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1 Further structural analysis of xylan showed that the esk1 mutation caused a specific reduction in 2-O- and 3-O-monoacetylation of xylosyl residues but not in 2,3-di-O-acetylation or 3-O-acetylation of xylosyl residues substituted at O-2 with glucuronic acid. hippuric acid trichome birefringence-like protein (DUF828) Arabidopsis thaliana
2 Together, these results demonstrate that ESK1 is a putative xylan acetyltransferase required for 2-O- and 3-O-monoacetylation of xylosyl residues and indicate the complexity of the biochemical mechanism underlying xylan O-acetylation. hippuric acid trichome birefringence-like protein (DUF828) Arabidopsis thaliana