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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| − | '''16 Jan 2013:''' ''Class I mannosidases × Williams<sup>2</sup> = 90<sup>th</sup> CAZypedia GH page.'' '''[[User:Rohan Williams|Rohan Williams]]''' and '''[[User:Spencer Williams|Spencer Williams]]''' completed the '''[[Glycoside Hydrolase Family 47]]''' page today to give CAZypedia its 90<sup>th</sup> [[:Category:Curator approved|Curator Approved]] GH page. '''[[GH47]]''' is particularly important because it contains alpha-1,2 mannosidases that are responsible for N-glycan processing in eukaryotes. Delineated by subfamily membership, these eukaryotic mannosidases function either in glycoprotein maturation or endoplasmic reticulum-associated degradation (ERAD). | + | '''16 Jan 2013:''' ''Class I mannosidases × Williams<sup>2</sup> = 90<sup>th</sup> CAZypedia GH page.'' '''[[User:Rohan Williams|Rohan Williams]]''' and '''[[User:Spencer Williams|Spencer Williams]]''' completed the '''[[Glycoside Hydrolase Family 47]]''' page today to give CAZypedia its 90<sup>th</sup> [[:Category:Curator approved|Curator Approved]] GH page. '''[[GH47]]''' is particularly important because it contains alpha-1,2 mannosidases that are responsible for N-glycan processing in eukaryotes. Delineated by subfamily membership, these eukaryotic mannosidases function either in glycoprotein maturation or endoplasmic reticulum-associated degradation (ERAD). Very few bacterial '''[[GH47]]''' members are known, in contrast, and their function(s) has not been widely studied. From a mechanistic perspective, '''[[GH47]]''' members are intriguing because the catalytic residues have not been unambiguously identified, despite high-resolution structure-function studies of these [[inverting]] enzymes. ''Check out the [[GH47]] to learn more!'' |
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'''14 Jan 2013:''' ''CAZypedia makes a contribution to MediaWiki community.'' We are proud to announce that [http://www.mediawiki.org/wiki/Extension:BiblioPlus BiblioPlus], an extension that provides automatic reference formatting to CAZypedia, has been officially accepted by the [http://www.mediawiki.org/wiki/Extension:BiblioPlus MediaWiki Extensions repository]. [http://www.mediawiki.org/wiki/Extension:BiblioPlus BiblioPlus] was coded by '''[[User:Karen Eddy|Karen Eddy]]''', a UBC computer science student working with '''[[User:Harry Brumer|Harry Brumer]]''', to resolve formatting issues with non-Western characters in PubMed data. [http://www.mediawiki.org/wiki/Extension:BiblioPlus BiblioPlus] is now available for anyone to use with any MediaWiki-based site to facilitate referencing journals and books. ''Thanks Karen, for all the hard work!'' | '''14 Jan 2013:''' ''CAZypedia makes a contribution to MediaWiki community.'' We are proud to announce that [http://www.mediawiki.org/wiki/Extension:BiblioPlus BiblioPlus], an extension that provides automatic reference formatting to CAZypedia, has been officially accepted by the [http://www.mediawiki.org/wiki/Extension:BiblioPlus MediaWiki Extensions repository]. [http://www.mediawiki.org/wiki/Extension:BiblioPlus BiblioPlus] was coded by '''[[User:Karen Eddy|Karen Eddy]]''', a UBC computer science student working with '''[[User:Harry Brumer|Harry Brumer]]''', to resolve formatting issues with non-Western characters in PubMed data. [http://www.mediawiki.org/wiki/Extension:BiblioPlus BiblioPlus] is now available for anyone to use with any MediaWiki-based site to facilitate referencing journals and books. ''Thanks Karen, for all the hard work!'' | ||
Revision as of 21:12, 16 January 2013
16 Jan 2013: Class I mannosidases × Williams2 = 90th CAZypedia GH page. Rohan Williams and Spencer Williams completed the Glycoside Hydrolase Family 47 page today to give CAZypedia its 90th Curator Approved GH page. GH47 is particularly important because it contains alpha-1,2 mannosidases that are responsible for N-glycan processing in eukaryotes. Delineated by subfamily membership, these eukaryotic mannosidases function either in glycoprotein maturation or endoplasmic reticulum-associated degradation (ERAD). Very few bacterial GH47 members are known, in contrast, and their function(s) has not been widely studied. From a mechanistic perspective, GH47 members are intriguing because the catalytic residues have not been unambiguously identified, despite high-resolution structure-function studies of these inverting enzymes. Check out the GH47 to learn more!
14 Jan 2013: CAZypedia makes a contribution to MediaWiki community. We are proud to announce that BiblioPlus, an extension that provides automatic reference formatting to CAZypedia, has been officially accepted by the MediaWiki Extensions repository. BiblioPlus was coded by Karen Eddy, a UBC computer science student working with Harry Brumer, to resolve formatting issues with non-Western characters in PubMed data. BiblioPlus is now available for anyone to use with any MediaWiki-based site to facilitate referencing journals and books. Thanks Karen, for all the hard work!
02 Dec 2012: Spencer does it again, twice. Spencer Williams has upgraded another two lexicon pages to Curator Approved status today. Have no idea what Oxazolinium ions and Oxocarbenium ions are, or why they're important in glycosidases? Check out these new pages!
20 Nov 2012: A growing lexicon, II: Spencer Williams has upgraded the Glycosyltransferases lexicon page to Curator Approved status today. This class of enzymes catalyzes the biosynthesis of the tremendous natural diversity of glycosides from activated sugar donor substrates and, as such, this page forms an essential part of CAZypedia's lexicon of terms and concepts. Thanks Spencer, for continuing to develop this resource!
16 Nov 2012: N-glycan deconstruction: There's been a flurry of activity on CAZypedia this past week; today, Al Boraston completed the Glycoside Hydrolase Family 125 page. GH125 was established last year based on a collaborative study between the Boraston and Vocadlo groups, which demonstrated that certain members from human bacterial pathogens can cleave alpha(1-6) mannosyl linkages typical of human N-glycans. Notably, GH125 members are also found in human gut symbiotic bacteria and pathogenic fungi, which underscores their potential biological importance in N-glycan deconstruction. Check out the GH125 page to read more about this new family, including a link to David and Al's seminal publication.
15 Nov 2012: A growing lexicon: Back in January of 2010, Wim Nerinckx compiled a monumental table on the orientation of the catalytic acid/base residue in over 70 GH families. Wim has now elaborated this page with an essential introduction to the important concept of Syn/anti lateral protonation in glycosidase catalysis, which was outlined in a seminal paper by Tom Heightman and Andrea Vasella in 1999. Now updated to Curator Approved from Under Construction status, this page forms a key part of CAZypedia's lexicon of terms and concepts.
12 Nov 2012: Three new GH families: Thanks to our colleagues in Japan, three pages on recently established glycoside hydrolase families have been completed and given Curator Approved status in CAZypedia today. The GH121 and GH127 family pages by Kiyotaka Fujita describe Bifidobacterium longum enzymes involved in plant hydroxyproline-rich glycoprotein (HRGP) deconstruction. The GH129 page by Hisashi Ashida describes another family of Bifidobacterial enzymes, which in this case, appear to be involved in mucin glycoprotein degradation. Special thanks go to Responsible Curator Shinya Fushinobu for organizing the production of these important new pages!
25 Oct 2012: A new GH family is born: Jean-Guy Berrin and his team at INRA in Marseille have recently unveiled a new glycoside hydrolase family, Glycoside Hydrolase Family 131, through elegant biochemical studies on a bi-modular β-glucanase from the fungus Podospora anserina. We are pleased to report that Jean-Guy has completed and given Curator Approved status to this fledgling CAZypedia page today, on which you can learn more about the INRA team's seminal work.
05 Sep 2012: Transglucosylases: The Glycoside Hydrolase Family 70 page by Magali Remaud-Simeon has been copy-edited by Responsible Curator Stefan Janecek and given Curator Approved status today. GH70 comprises a family of enzymes with the notable ability to build high molecular weight α-glucan polysaccharides from sucrose as a glucosyl donor substrate. Depending the particular enzyme, α-1,2-; α-1,3-; α-1,4-; and/or α-1,6-linked glucans can be produced, which have applications in food, pharmaceutical, and fine chemical industries. In addition, biofilms of α-1,3-glucans produced by the GH70 enzymes of oral bacteria are also implicated in the formation of dental caries (cavities). Learn more about this interesting family of CAZymes here!