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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23 June 2013: Yet another Lexicon page: Spencer Williams updated the Lexicon page on Phosphorylases today to Curator Approved status, bring the number of completed Lexicon pages to 20. Phosphorylases catalyze glycosidic bond cleavage through nucleophilic substitution with phosphate (PO4--), and play important roles in, for example, storage polysaccharide breakdown by generating glucose-1-phosphate as a precursor to glycolysis. Notably, phosphorylases based on both glycoside hydrolase and glycosyltransferase protein folds are known. Read more about this important class of carbohydrate-active enzymes here.
Attention CAZymologists! Upcoming conferences:
- Registration is now open for the 2013 Gordon Research Conference on Cellulosomes, Cellulases & Other Carbohydrate Modifying Enzymes. Follow the link for more information, including the schedule of world-leading speakers. Junior scientists are especially encouraged to attend the affiliated Gordon Research Seminar.
- Fifth Symposium on the Alpha-Amylase Family - ALAMY_5, October 20-24, Smolenice Castle, Slovakia.
22 May 2013: Our very first CBM page!: Elizabeth Ficko-Blean and Alisdair Boraston finalized CAZypedia's first Carbohydrate Binding Module Family page, CBM32, today. This ushers in a new phase in CAZypedia's development, and we are looking forward to the continued evolution of this group of pages on these non-catalytic, substrate-binding, CAZyme-associated protein modules.
2 May 2013: Adding on to the Lexicon: Today Spencer Williams added the finishing touches to the Lexicon page on Transglycosylases. Transglycosylation - the ability to non-hydrolytically rearrange glycosidic bonds between one or more substrates - is a feature of many Glycoside hydrolases, especially those which use the retaining mechanism. In such enzymes, the covalent glycosyl-enzyme reaction intermediate can be intercepted by either water (yielding hydrolysis) or a sugar "acceptor" substrate (yielding transglycosylation). Although transglycosylation is generally a side activity of retaining enzymes, a handful are naturally very predominant Transglycosylases. See the Lexicon page to learn more, including specific examples!