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.
Template:News
12 May 2011: A new page on a new-ish family: Author and Responsible Curator Satoshi Kaneko completed the Glycoside Hydrolase Family 115 page today. GH115 contains microbial alpha-glucuronidases, which are involved the cleavage of D-glucuronic acid and 4-O-methyl-D-glucuronic acid sidechains from xylans. Remarkably, GH115 enzymes can release these monosaccharides from intact polymer chains, which is rather rare for exo-acting enzymes, and contrasts them with glucuronidases from GH67. Although this regiospecific activity has been known since the last millenium, it was only in 2009 that these particular enzymes nucleated their own GH family.
09 May 2011: It's a big news day here at CAZypedia. We are proud to announce that three distinct glycoside hydrolase family pages have been Curator Approved today:
- Glycoside Hydrolase Family 74 (written by Katsuro Yaoi and Takuya Ishida, and curated by Katsuro Yaoi) is a family predominantly comprised of endo-glucanases that are specific for the plant polysaccharide xyloglucan (true xyloglucanases).
- Glycoside Hydrolase Family 95 (written and curated by Takane Katayama) is a family of 1,2-α-L-fucosidases, members of which cleave human milk oligosaccharides, blood group glycoconjugates, and/or xyloglucan oligosaccharides.
- Glycoside Hydrolase Family 117 (written by Etienne Rebuffet and curated by Mirjam Czjzek) is a small, newly created family of α-1,3-L-(3,6-anhydro)-galactosidases (neoagarobiose hydrolases), which catalyze the final step in the degradation of agars from red macroalgae in the marine environment.
We would like to express our sincere thanks to our Japanese and French colleagues for these important contributions to CAZypedia. Links to these families will be included in the next public update of the CAZy database (expected soon!).
Special thanks also go to Etienne for updating the Glycoside Hydrolase Family 82 page, including a very cool animated image that highlights enzyme domain movement during substrate binding - CAZypedia really is a living resource that can be continually improved with the latest knowledge.
28 April 2011: More on α-glucoside cleavage: Author and Responsible Curator Takashi Tonozuka recently completed the Glycoside Hydrolase Family 63 page, which has been updated to Curator Approved status today. GH63 is especially notable as it contains the eukaryotic "processing α-glucosidase I enzymes," which are essential for N-glycan trimming during glycoprotein maturation. Takashi Tonozuka's group has done seminal structural elucidation work in this family, and we very much appreciate his contribution to CAZypedia, especially during these tough times in Japan.
21 March 2011: A new page on the equinox (as we thaw-out and welcome the sun back to the Baltic region): Responsible Curator Anna Kulminskaya today approved the Glycoside Hydrolase Family 35 page, which was written by Anna, with input on the 3-D structure section from Mirko Maksimainen and Juha Rouvinen. GH35 is a family of β-galactosidases from diverse organisms that display a range of bond specificities. Only very few tertiary structures have been solved in this family, to which the Russian and Finnish groups have made seminal contributions.
28 February 2011: Hexosaminidases!: The Glycoside Hydrolase Family 20 and Glycoside Hydrolase Family 84 pages, which were completed last week by Author Ian Greig and approved by Responsible Curator David Vocadlo, have today been cross-linked from the CAZy database (look out for the next public release). GH20 is of significant medical relevance, as it contains the human enzymes HexA and HexB, deficiencies of which case Tay-Sachs disease and Sandhoff diseases, respectively. GH84 is similarly important in the context of cell and organism biology, as this family contains human OGA (HexC, MGEA5, O-GlcNAcase), a nuclear and cytoplasmic enzyme that is responsible for dynamic modulation of β-linked O-GlcNAc residues linked to serine and threonine residues. O-GlcNAc'ylation of specific protein residues has in some cases been found to be reciprocal to phosphorylation and, accordingly, has implicated O-GlcNAc in diverse cellular processes and disease states.