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'''16 Jan 2013:''' ''Class I mannosidases &times; 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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'''2 May 2024:''' ''CBDs I to X... A major milestone!'' '''CBM families 1 to 10 are now complete!''' These are the old CBD (cellulose-binding domain) families, which used to have roman numerals as part of their nomenclature. A special thank you to all the authors and responsible curators who have contributed to this major milestone. Go have a peek at each of these old school families on their respective ''CAZypedia'' pages: '''[[CBM1]], [[CBM2]], [[CBM3]], [[CBM4]], [[CBM5]], [[CBM6]], [[CBM7]], [[CBM8]], [[CBM9]], and [[CBM10]]'''.
 
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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!''
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'''11 February 2024:''' ''A "BLAST" from the past, with a fresh update.'' [[Author]] '''[[User:Eduardo Moreno Prieto|Eduardo Moreno Prieto]]''' composed a new page on '''[[Glycoside Hydrolase Family 119]]''',a family of bacterial amylases, which was [[Curator Approved]] by '''[[User:Stefan Janecek|Stefan Janecek]]''' and '''[[User:Bernard Henrissat|Bernard Henrissat]]''' todayThe first member of '''[[GH119]]''' was characterized in 2006, and through sequence analysis with [[GH57]] members, [[User:Stefan Janecek|Janeček]] and Kuchtová predicted the active-site residues in 2012. Over a decade later, '''[[User:Eduardo Moreno Prieto|Eduardo]]''', '''[[User:Bernard Henrissat|Bernard]]''', and colleagues finally provided critical experimental support for these predictions''Learn more about this history, and especially the relationship between '''[[GH119]]''' and '''[[GH57]]''', in CAZypedia.''
 
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'''02 Dec 2012:''' ''Spencer does it again, twice.'' '''[[User:Spencer Williams|Spencer Williams]]''' has upgraded another two [[lexicon]] pages to [[:Category:Curator approved|Curator Approved]] status today.  Have no idea what '''[[Oxazolinium ion]]s''' and '''[[Oxocarbenium ion]]s''' are, or why they're important in [[glycosidase]]s?  ''Check out these new pages!''
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'''3 February 2024:''' ''A new family of beta-1,2-glucan-cyclizing enzymes.'' A page on the (currently) newest GH family, '''[[Glycoside Hydrolase Family 189]]''', was completed today by [[Author]]s '''[[User:Tomoko Masaike|Tomoko Masaike]]''', '''[[User:Masahiro Nakajima|Masahiro Nakajima]]''', and '''[[User:Nobukiyo Tanaka|Nobukiyo Tanaka]]''' ([[User:Masahiro Nakajima|Masahiro Nakajima]] is the [[Responsible Curator]]). '''[[GH189]]''' is a family of bacterial transglycosylases that comprise a critical domain in cyclic beta-1,2-glucan synthase (CGS), because this domain is responsible for the final cyclization step during the biosynthesis of these key effector molecules.  The discovery of '''[[GH189]]''' builds on similarly exciting work by these authors and their colleagues on beta-1,2-glucan hydrolases in [[GH144]] and [[GH162]], which share a common protein fold with '''[[GH189]]''', but have distinct mechansims. ''Check out the '''[[GH189]]''', [[GH144]], and [[GH162]] pages to learn more about this breakthrough work on beta-1,2-glucan-active enzymes!''
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'''20 Nov 2012:''' ''A growing lexicon, II:'' '''[[User:Spencer Williams|Spencer Williams]]''' has upgraded the '''[[Glycosyltransferases]]''' [[lexicon]] page to [[:Category:Curator approved|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 [[User:Spencer Williams|Spencer]], for continuing to develop this resource!''
 
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'''16 Nov 2012:''' ''N-glycan deconstruction:'' There's been a flurry of activity on ''CAZypedia'' this past week; today, '''[[User:Al Boraston|Al Boraston]]''' completed the '''[[Glycoside Hydrolase Family 125]]''' page.  '''[[GH125]]''' was established last year based on a collaborative study between the '''[[User:Al Boraston|Boraston]]''' and '''[[User:David Vocadlo|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 '''[[User:David Vocadlo|David]]''' and '''[[User:Al Boraston|Al's]]''' seminal publication.''
 
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'''15 Nov 2012:''' ''A growing lexicon:'' [[News|Back in January of 2010]], '''[[User:Wim Nerinckx|Wim Nerinckx]]''' compiled a monumental table on the [[Syn/anti lateral protonation|orientation of the catalytic acid/base residue]] in over 70 GH families. '''[[User:Wim Nerinckx|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 [[:Category:Curator approved|Curator Approved]] from [[:Category:Under construction|Under Construction]] status, this page forms a key part of ''CAZypedia's'' [[lexicon]] of terms and concepts.
 
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'''12 Nov 2012:''' ''<u>Three</u> new GH families:'' Thanks to our colleagues in Japan, three pages on recently established glycoside hydrolase families have been completed and given [[:Category:Curator approved|Curator Approved]] status in ''CAZypedia'' today.  The '''[[GH121]]''' and '''[[GH127]]''' family pages by '''[[User:Kiyotaka Fujita|Kiyotaka Fujita]]''' describe ''Bifidobacterium longum'' enzymes involved in plant hydroxyproline-rich glycoprotein (HRGP) deconstruction.  The '''[[GH129]]''' page by '''[[User:Hisashi Ashida|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]] '''[[User:Shinya Fushinobu|Shinya Fushinobu]]''' for organizing the production of these important new pages!
 
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'''25 Oct 2012:''' ''A new GH family is born:'' '''[[User:Jean-Guy Berrin|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 &beta;-glucanase from the fungus ''Podospora anserina''.  We are pleased to report that '''[[User:Jean-Guy Berrin|Jean-Guy]]''' has completed and given [[:Category:Curator approved|Curator Approved]] status to this fledgling ''CAZypedia'' page today, on which you can [[Glycoside Hydrolase Family 131|learn more about the INRA team's seminal work]].
 
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'''05 Sep 2012:''' ''Transglucosylases:'' The '''[[Glycoside Hydrolase Family 70]]''' page by '''[[User:Magali Remaud-Simeon|Magali Remaud-Simeon]]''' has been copy-edited by [[Responsible Curator]] '''[[User:Stefan Janecek|Stefan Janecek]]''' and given [[:Category:Curator approved|Curator Approved]] status today.  '''[[GH70]]''' comprises a family of enzymes with the notable ability to build high molecular weight &alpha;-glucan polysaccharides from sucrose as a glucosyl donor substrate.  Depending the particular enzyme, &alpha;-1,2-; &alpha;-1,3-; &alpha;-1,4-; and/or &alpha;-1,6-linked glucans can be produced, which have applications in food, pharmaceutical, and fine chemical industries.  In addition, biofilms of &alpha;-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 [[Glycoside Hydrolase Family 70|here]]!
 
 
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Latest revision as of 08:08, 2 May 2024

2 May 2024: CBDs I to X... A major milestone! CBM families 1 to 10 are now complete! These are the old CBD (cellulose-binding domain) families, which used to have roman numerals as part of their nomenclature. A special thank you to all the authors and responsible curators who have contributed to this major milestone. Go have a peek at each of these old school families on their respective CAZypedia pages: CBM1, CBM2, CBM3, CBM4, CBM5, CBM6, CBM7, CBM8, CBM9, and CBM10.


11 February 2024: A "BLAST" from the past, with a fresh update. Author Eduardo Moreno Prieto composed a new page on Glycoside Hydrolase Family 119,a family of bacterial amylases, which was Curator Approved by Stefan Janecek and Bernard Henrissat today. The first member of GH119 was characterized in 2006, and through sequence analysis with GH57 members, Janeček and Kuchtová predicted the active-site residues in 2012. Over a decade later, Eduardo, Bernard, and colleagues finally provided critical experimental support for these predictions. Learn more about this history, and especially the relationship between GH119 and GH57, in CAZypedia.


3 February 2024: A new family of beta-1,2-glucan-cyclizing enzymes. A page on the (currently) newest GH family, Glycoside Hydrolase Family 189, was completed today by Authors Tomoko Masaike, Masahiro Nakajima, and Nobukiyo Tanaka (Masahiro Nakajima is the Responsible Curator). GH189 is a family of bacterial transglycosylases that comprise a critical domain in cyclic beta-1,2-glucan synthase (CGS), because this domain is responsible for the final cyclization step during the biosynthesis of these key effector molecules. The discovery of GH189 builds on similarly exciting work by these authors and their colleagues on beta-1,2-glucan hydrolases in GH144 and GH162, which share a common protein fold with GH189, but have distinct mechansims. Check out the GH189, GH144, and GH162 pages to learn more about this breakthrough work on beta-1,2-glucan-active enzymes!