Pectic substances from soybean cell walls distinguish themselves from other plant cell wall pectins

The uncommon structural features of soybean cell wall pectic substances explain their resistance to degradation by enzymes generally used to degrade this kind of polymers, and indicates that a search for new enzymes is required to enable enzymatic modification of these polysaccharide

Identification of a novel group of putative Arabidopsis thaliana beta-(1,3)-galactosyltransferases

The original publication can be found at www.springerlink.comTo begin biochemical and molecular studies on the biosynthesis of the type II arabinogalactan chains on arabinogalactan-proteins (AGPs), we adopted a bioinformatic approach to identify and systematically characterise the putative galactosyltransferases (GalTs) responsible for synthesizing the β-(1,3)-Gal linkage from CAZy GT-family-31 from Arabidopsis thaliana. These analyses confirmed that 20 members of the GT-31 family contained domains/motifs typical of biochemically characterised β-(1,3)-GTs from mammalian systems. Microarray data confirm that members of this family are expressed throughout all tissues making them likely candidates for the assembly of the ubiquitously found AGPs. One member, At1g77810, was selected for further analysis including location studies that confirmed its presence in the Golgi and preliminary enzyme substrate specificity studies that demonstrated β-(1,3)-GalT activity. This bioinformatic/molecular study of CAZy GT-family-31 was validated by the recent report of Strasser et al. (Plant Cell 19:2278–2292, 2007) that another member of this family (At1g26810; GALT1) encodes a β-(1,3)-GalT involved in the biosynthesis of the Lewis a epitope of N-glycans in Arabidopsis thaliana.Yongmei Qu, Jack Egelund, Paul R. Gilson, Fiona Houghton, Paul A. Gleeson, Carolyn J. Schultz and Antony Baci