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15 May 2020: More on beta(1,3)-glucanases. The Glycoside Hydrolase Family 64 page, Authored by Julie Grondin, was completed and Curator Approved today. GH64 comprises a group of laminaripentaose-producing β-1,3-glucanases, primarily from bacteria.The archetype of this family was originally cloned from a Streptomyces species in the late 1990's and was the subject of mechanistic and structural analysis through the first decade of the new millenium. Notably, analysis by a team led by Bernard Henrissat defined that this enzyme, and thus family, uses an inverting mechanism, further disntiguishing it from well-known retaining beta(1,3)-glucanases of GH16, GH17, and others, including the recently described GH158 reported below. Read more about the unique Glycoside Hydrolase Family 64 here.
11 May 2020: Three more from the gut. Alan Cartmell completed no less than three new Glycoside Hydrolase Family pages on this day. Glycoside Hydrolase Family 137, Glycoside Hydrolase Family 140, and Glycoside Hydrolase Family 145 were all created from a series of studies of Polysacchardie Utilization Loci from human gut bacteria by Harry Gilbert's group, to which Alan contributed defining crystallography. Alan has also taken over the duty of Responsible Curator of these pages following the retirement of the venerable Professor Gilbert, one of CAZypedia's founding Senior Curators. Read more about the substrate specificity and structural biology of these three diverse families on their corresponding pages.
6 May 2020: CE #1! The first Carbohydrate Esterase Family page in the series, CE1, was Curator Approved today. Authored by Casper Wilkens, the Carbohydrate Esterase Family 1 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 CE1 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.