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.
*
Consider attending the 15th Carbohydrate Bioengineering Meeting in Ghent, 5-8 May 2024.

Difference between revisions of "Template:News"

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'''11 October 2017:''' ''Ten years of CAZypedia:'' We are proud to announce the publication of a [https://academic.oup.com/glycob/article-lookup/doi/10.1093/glycob/cwx089 new article in ''Glycobiology''] in celebration of ''CAZypedia's'' tenth anniversary online. This article was written on behalf of all of present and future '''[[:Category:Contributors|Contributors]]''' by Curators [[User:Harry Brumer|Harry Brumer]] and [[User:Spencer Williams|Spencer Williams]], with input from a number of key individuals involved in the genesis of ''CAZypedia'' (''see the [https://academic.oup.com/glycob/article-lookup/doi/10.1093/glycob/cwx089 Acknowledgements section] for full details''). A final post-print version of the manuscript will be [http://hdl.handle.net/2429/63428 freely available].  ''Thanks to the hard work of a multitude of [[:Category:Contributors|Contributors]], ''CAZypedia'' is a successful example of community-driven, expert-based biocuration.  We look forward to the continued development of this resource over the next ten years!''
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'''10 September 2017:''' ''Sussing-out starch recognition in CBM58:'' We are excited to report that '''[[User:Nicole Koropatkin|Nicole Koropatkin]]''' has completed the '''[[Carbohydrate Binding Module Family 58]]''' page today.  [[CBM58]] constitutes a comparatively small family of CBMs found in bacteria in the phylum Bacteroidetes, including key members of the human gut microbiota such as ''Bacteroides thetaiotaomicron''.  Within these bacteria, [[CBM58]] modules are found inserted within the [[GH13]] catalytic module of SusG, the essential outer-membrane-bound amylase of the starch utilization system (sus).  [[User:Nicole Koropatkin|Nicole’s]] seminal structural biology has defined the family and provided insight into the recognition of amylose helices by [[CBM58]] members in SusG homologs.  ''Read more about this fascinating system [[Carbohydrate Binding Module Family 58|here]].''       
 
'''10 September 2017:''' ''Sussing-out starch recognition in CBM58:'' We are excited to report that '''[[User:Nicole Koropatkin|Nicole Koropatkin]]''' has completed the '''[[Carbohydrate Binding Module Family 58]]''' page today.  [[CBM58]] constitutes a comparatively small family of CBMs found in bacteria in the phylum Bacteroidetes, including key members of the human gut microbiota such as ''Bacteroides thetaiotaomicron''.  Within these bacteria, [[CBM58]] modules are found inserted within the [[GH13]] catalytic module of SusG, the essential outer-membrane-bound amylase of the starch utilization system (sus).  [[User:Nicole Koropatkin|Nicole’s]] seminal structural biology has defined the family and provided insight into the recognition of amylose helices by [[CBM58]] members in SusG homologs.  ''Read more about this fascinating system [[Carbohydrate Binding Module Family 58|here]].''       
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'''10 April 2017:''' ''A classic GH family:'' The '''[[Glycoside Hydrolase Family 22]]''' page was completed today by '''[[User:Spencer Williams|Spencer Williams]]''', with editorial input from [[Responsible Curator]] '''[[User:David Vocadlo|David Vocadlo]]'''.  '''[[GH22]]''' contains the classic bacterial peptidoglycan hydrolase, hen egg-white lysozyme (HEWL), the first enzyme for which the three-dimensional structure was solved (reported in 1965).  Moreover, seminal enzyme-carbohydrate complex structures have made HEWL a paradigm for glycosidases that operate through the [[classical Koshland retaining mechanism]].  Although the nature of the reaction intermediate remained contentious for many years since the original proposal of an oxacarbenium ion-carboxylate pair, a definitive study by  [[User:David Vocadlo|Vocadlo]], [[User:Gideon Davies|Davies]], Laine, and [[User:Steve Withers|Withers]] resolved the covalent nature of the glycosyl-enzyme HEWL in 2001, thus bringing mechanistic understanding of this classic enzyme in concordance with other [[retaining]] GH families.  The lysozyme fold of HEWL defines the archetype for other hexosaminidases (i.e. those of [[GH19]] and [[GH23]]) and the non-catalytic alpha-lactalbumins, and this fold notably has also been observed in recently emergent families of cellulases ([[GH124]]) and mannanases ([[GH134]]).  ''Find out more about this classic GH family  [[Glycoside Hydrolase Family 22|here]]!''
 
 
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Revision as of 11:11, 6 November 2017

11 October 2017: Ten years of CAZypedia: We are proud to announce the publication of a new article in Glycobiology in celebration of CAZypedia's tenth anniversary online. This article was written on behalf of all of present and future Contributors by Curators Harry Brumer and Spencer Williams, with input from a number of key individuals involved in the genesis of CAZypedia (see the Acknowledgements section for full details). A final post-print version of the manuscript will be freely available. Thanks to the hard work of a multitude of Contributors, CAZypedia is a successful example of community-driven, expert-based biocuration. We look forward to the continued development of this resource over the next ten years!


10 September 2017: Sussing-out starch recognition in CBM58: We are excited to report that Nicole Koropatkin has completed the Carbohydrate Binding Module Family 58 page today. CBM58 constitutes a comparatively small family of CBMs found in bacteria in the phylum Bacteroidetes, including key members of the human gut microbiota such as Bacteroides thetaiotaomicron. Within these bacteria, CBM58 modules are found inserted within the GH13 catalytic module of SusG, the essential outer-membrane-bound amylase of the starch utilization system (sus). Nicole’s seminal structural biology has defined the family and provided insight into the recognition of amylose helices by CBM58 members in SusG homologs. Read more about this fascinating system here.