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6 May 2020: CE #1! The first Carbohydrate Esterase Family page in the series, [[[CE1]]], was Curator Approved today. Authored by Casper Wilkens, the [[[CE1]]] page describes an old family of carbohydrate-specific and other esterases, members of which were identified through classical biochemistry, before the present age of easy gene cloning and sequencing. Carbohydrate-active members of Carbohydrate Esterase Family 1 include acetyl xylan esterases, cinnamoyl esterases, and feruloyl esterases responsible for hydrolyzing pendant acyl groups from plant cell wall matrix glycans (hemicelluloses). Read more about the long history of Carbohydrate Esterase Family 1 here.
10 April 2020: Yet another new one from the gut. Today, Author Kazune Tamura completed the Glycoside Hydrolase Family 158 page. GH158 emerged in 2019 from a high-throughput biochemical survey of sequences identified as distantly related to glycoside hydrolases by the CAZy team, who first demonstrated endo-beta(1,3)-glucanase activity for the founding member of the family from the human gut bacterium Victivallis vadensis. Contemporaneously, analysis of homolgos from human gut Bacteroides species by Guillaume Dejean and Kazune Tamura resolved details of the specificity, mechanism, and tertiary structure of GH158 members in Polysaccharide Utilization Loci. Read about the detailed history and juicy details of this new GH family here.
8 April 2020: Another new one from the gut. The Glycoside Hydrolase Family 164 page, which was authored by Zachary Armstrong, was upgraded to Curator Approved status by Responsible Curator Gideon Davies today. Glycoside Hydrolase Family 164 is yet another newly discovered GH family from a human gut bacterium - this time through a large-scale effort by teams at AFMB and CERMAV spearheaded by Bernard Henrissat. The founding member of GH164 is a beta-mannosidase from Bacteroides salyersiae, on which Zach and Gideon performed a classic mechanistic and structural analysis to define the central aspects of catalysis in this new family. Read more about this new - and currently tiny - GH family here.
14 February 2020: A rose by any other name would smell as sweet. The human gut bacterium Roseburia intestinalis provides a Curator Approved Carbohydrate Binding Module Family 86 page as a special Valentine Day's gift. CBM86 members are structurally located at the N-termini of GH10 xylanase polypeptides. Roseburia intestinalis certainly enjoys the sugary xylans it encounters in the dietary tract as a carbon source and likely uses the CBM86 modules to enhance xylan capture through improved xylan affinity for the xylanase enzymes. The CBM86 page was written in record time by Maria Louise Leth with Maher Abou Hachem acting as Responsible Curator. Read more about this 'rosy' xylan-binding family here.