CAZypedia needs your help! We have many unassigned GH, PL, CE, AA, GT, and CBM pages in need of Authors and Responsible Curators.
Scientists at all career stages, including students, are welcome to contribute to CAZypedia. Read more here, and in the 10th anniversary article in Glycobiology.
New to the CAZy classification? Read this first.
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Consider attending the 15th Carbohydrate Bioengineering Meeting in Ghent, 5-8 May 2024.
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4 January 2024: More "Fun" from the sea. Today, Yaoguang Chang Curator Approved the Glycoside Hydrolase Family 187 page Authored by Jingjing Shen. The founding member of GH187 is the alpha-1,3-L-fucanase ("Fun187A") the marine bacterium Wenyingzhuangia aestuarii, which recognizes a specific sulfated motif in seaweed fucans. GH187 is a small family (<50 members) and there remains much to elucidate regarding catalytic mechanism and enzyme structure. Interest in CAZymes active on marine biomass continues to grow, and we welcome this expansion in CAZypedia. Learn more about GH187 here!
17 December 2023: Redox-assisted glycoside hydrolysis. Just before the turn of the new year, Spencer Williams completed the Glycoside Hydrolase Family 188 page. GH188 is the latest representative of a growing number of Glycoside Hydrolase families, including GH4, GH109, GH177, and GH179, which use an NAD-dependent oxidation-elimination-addition-reduction cycle to cleave glycosidic bonds. First established ca. 20 years ago in GH4, this mechanism is therefore distinct from the canonical Koshland mechanisms of glycoside hydrolysis. Notably, because oxidation occurs at C-3 of the sugar ring, followed by elimination at C-1, these enzymes can cleave both alpha- and beta-glycosides! Recently, Spencer, Ethan Goddard-Borger, and Gideon Davies showed that NAD-dependent hydrolysis also extends to sulfoquinovoside hydrolysis by bacterial GH188 members, complementing canonical sulfoquinovosidases in GH31. Read more about these remarkable enzymes here!
16 August 2023: An oldie but a goodie. The page for CBM9, one of the original founding top 10 Carbohydrate Binding Module Families, has been completed by Johan Larsbrink, who multitasked as both Author and Responsible Curator. CBM9 members are often found in ultra-multimodular, xylan deconstructing, bacterial enzymes, and their cellulose-binding functionality has been exploited as affinity tags in recombinant protein purifications. Read more on this historically important CBM family here!
25 June 2023: Another one from the capybara gut. We're pleased to announce that the Glycoside Hydrolase Family 173 page, written by Authors Clelton Aparecido dos Santos and Gabriela Felix Persinoti was Curator Approved by Mario Murakami today. This new family of beta-galactosidases was created through the same study of the capybara gut metagenome by the Murakami group that led to the creation of family CBM89 (see the June 22nd News item). GH173 appears to be distantly related to GH5 and GH30 in Clan GH-A, yet there remain many unknowns about this family and its founding member - read more here!
23 June 2023: Human milk oligosaccharide metabolism. Author Chihaya Yamada and Responsible Curator Shinya Fushinobu upgraded the Glycoside Hydrolase Family 136 page to Curator Approved status today. GH136 is a family of bacterial lacto-N-biosidases that release lacto-N-biose I and lactose from lacto-N-tetraose, the main component of human milk oligosaccharides. These enzymes have a comparatively rare right-handed beta helix fold that more typical of pectin-active PLs and GHs. Read more about these interesting enzymes and their role in the human gut microbiota here!
22 June 2023: These CBMs are sizeable! The recently discovered xylan-binding CBM89 family, originating from the capybara gut microbiota, is described by Authors Mariana Abrahão Bueno de Morais and Gabriela Felix Persinoti. Mario Murakami acted as Responsible Curator on the page. CBM89 members are 600 - 1000 amino acids long which puts them in the upper echelons of CBM sizes - just as the capybara is to the rodent order. You can check out the write up on these unusually large CBMs on their CBM89 CAZypedia page.