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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Revision as of 09:13, 19 January 2010 by Harry Brumer (talk | contribs) (Undo revision 3561 by Harry Brumer (Talk))
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19 January 2010: Glycoside Hydrolase Family 58, which contains the E. coli bacteriophage tailspike endo-sialidases, has now been given Curator Approved status by author and curator Warren Wakarchuk. This is the second page by Warren, who did GH101 back in the autumn of 2009.


16 January 2010: Gerlind Sulzenbacher has completed a CAZypedia page on the α-L-fucosidase family GH29, which has just been approved by Responsible Curator Steve Withers. GH29 is particularly notable as it contains human α-fucosidase A1 (FucA1), defects in which give rise to the lysosomal storage disease fucosidosis.


15 January 2010: The Glycoside Hydrolase Family 57 has now been finished and given "Curator Approved" status by Stefan Janecek. This is CAZypedia's second page on starch-active enzymes, following Pedro Coutinho's GH15 contribution (see News, Nov. 6, 2009).


12 January 2010: Wim Nerinckx has just completed the herculean task of compiling an updated table on the orientation of the catalytic acid/base residue (syn vs. anti protonation) in all GH families, where known. Look out for a full lexicon entry by Wim and Spencer Williams soon!


11 January 2010: CAZypedia proudly announces our second page of the new year: Mirjam Czjzek (Station Biologique de Roscoff, France) and Wim Van den Ende (KULeuven, Belgium) have just completed the Glycoside Hydrolase Family 32 page!


04 January 2010: CAZypedia proudly announces our first page of the new year: Glycoside Hydrolase Family 92 by Prof. Harry Gilbert, which is based on work very recently published in Nature Chemical Biology.


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