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.

Difference between revisions of "Template:News"

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'''6 August 2020:''' ''A beta-1,3-glucanase family with a deep history:'' '''[[User:Julie Grondin|Julie Grondin's]]''' '''[[Glycoside Hydrolase Family 81]]''' page was [[Curator Approved]] by '''[[User:Al Boraston|Al Boraston]]''' today.  '''[[GH81]]''' has a long history of discovery and mechanistic study, including by original CAZypedian and [https://www.grc.org/carbohydrate-active-enzymes-for-glycan-conversions-conference/default.aspx Cellulase/CAZyme GRC co-founder] '''[[User:David Wilson|David Wilson]]''' and co-workers.  By capturing a phenomenal number of oligosaccharide complexes, '''[[User:Al Boraston|Al's]]''' group has recently provided detailed molecular description of how enzymes in this family specifically recognize the helical structure adopted by beta-1,3-glucans. ''Be sure to check out the [[Glycoside Hydrolase Family 81|GH81 page]] to get the full history of the contributions of a number of groups world-wide to our knowledge of this family.''
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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]]''' today.  The 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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'''23 July 2020:''' ''Another CE family page from our friends at WLU!'' The '''[[Carbohydrate Esterase Family 7]]''' page was finalized and promoted to [[Curator Approved]] status today.  '''[[User:Joel Weadge|Joel Weadge]]''' and '''[[User:Joel Weadge|Michael Suits]]''' have been leading the completion of a bunch of CE pages with the help of keen students from Wilfred Laurier University (see [[CE3]], [[CE4]], and [[CE9]]). This time, '''[[User:Emily Rodriguez|Emily Rodriguez]]''' produced the '''[[CE7]]''' page, which encompasses acetyl xylan esterases and cephalosporin-C deacetylases. ''Learn more about the specificity, mechanism, and three-dimensional structure of CE7 enzymes [[Carbohydrate Esterase Family 7|here]].''  
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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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'''4 January 2024:''' ''CBM99, CBM100 and CBM101 in one fell swoop!'' Three new CBM families have been added to the ''CAZypedia'' repertoire. Though the families differ in their glycan targets, they share the interesting function of binding to highly complex sulfated marine polymers. '''[[User:Yaoguang Chang|Yaoguang Chang]]''' acted as [[Responsible Curator]] on all three pages. '''[[User:Xuanwei Mei|Xuanwei Mei]]''' [[author]]ed the [[CBM99]] and [[CBM101]] red algal specific pages and '''[[User:Guanchen Liu|Guanchen Liu]]''' authored the [[CBM100]] glycosaminoglycan specific page. ''Learn more about [[CBM99]], [[CBM100]] and [[CBM101]] on their respective pages!''  
  
 
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'''19 June 2020:''' ''Three additional alginate lyase families!'' The number of PL family pages in ''CAZypedia'' continues to grow with the promotion of the '''[[Polysaccharide Lyase Family 6]]''', '''[[Polysaccharide Lyase Family 15]]''', and '''[[Polysaccharide Lyase Family 17]]''' pages to [[Curator Approved]] status today.  We thank '''[[User:Emil Stender|Emil G.P. Stender]]''' for his hard work in tackling this trifecta of bacterial alginate lyase families (including some heparin/heparan sulfate lyases from the human gut microbiota in '''[[PL15]]'''), which were vetted [[Responsible Curator]] '''[[User:Birte Svensson|Birte Svensson]]'''.  ''Dig into the details of these families on the '''[[PL6]]''', '''[[PL15]]''', and '''[[PL17]]''' pages, in comparison with the recently completed '''[[PL7]]''' page (see previous news item, below).''  
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'''4 January 2024:''' ''More "Fun" from the sea.'' Today, '''[[User:Yaoguang Chang|Yaoguang Chang]]''' [[Curator Approved]] the '''[[Glycoside Hydrolase Family 187]]''' page [[Author]]ed by '''[[User:Jingjing Shen|Jingjing Shen]]'''. The founding member of '''[[GH187]]''' is the alpha-1,3-L-fucanase ("Fun187A") the marine bacterium ''Wenyingzhuangia aestuarii'', which recognizes a specific sulfated motif in sea cucumber fucans.  '''[[GH187]]''' is a small family (<50 members) and there remains much to elucidate regarding catalytic mechanism and enzyme structure. Interest in CAZymes active on marine biomass continues to grow, and we welcome this expansion in ''CAZypedia''. ''Learn more about '''[[GH187|GH187 here!]]'''''
 
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'''17 June 2020:''' ''PLs from the sea.'' The '''[[Polysaccharide Lyase Family 7]]''' page, which was written by '''[[User:Nadine Gerlach|Nadine Gerlach]]''', was promoted to completed by [[Curator Approved]] status today by '''[[User:Jan-Hendrik Hehemann|Jan-Hendrik Hehemann]]'''. The founding member of '''[[PL7]]''', an alginate lyase, was characterized way back in 1993 by a team notably including CAZypedian [[User:Gurvan Michel|Gurvan Michel]].  Alginate is heteropolysaccharide from brown algae and mucoid bacteria, consisting of beta-{{Smallcaps|d}}-mannuronate (M) and alpha-{{Smallcaps|l}}-guluronate (G) residues in varying ratios and intra-chain distributions, depending on the source.  As a result, '''[[PL7]]''' members exhibit mannuronate, guluronate, or mixed link specificity. ''Read more about the deep history of enzymolgoy and structural biology of PL7 [[Polysaccharide Lyase Family 7|here]], including seminal work by '''[[User:Jan-Hendrik Hehemann|Jan-Hendrik]]''' showing the horizontal gene transfer of these enzymes into the human gut microbiota and other marine bacteria.''  
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'''17 December 2023:''' ''Redox-assisted glycoside hydrolysis, redux.'' Just before the turn of the new year, '''[[User:Spencer Williams|Spencer Williams]]''' completed the '''[[Glycoside Hydrolase Family 188]]''' page. '''[[GH188]]''' is the latest representative of a growing number of [[Glycoside hydrolases|Glycoside Hydrolase]] families, including [[GH4]], [[GH109]], [[GH177]], and [[GH179]], which use an [[NAD-dependent hydrolysis|NAD-dependent]] oxidation-elimination-addition-reduction cycle to cleave glycosidic bonds. First established ca. 20 years ago in [[GH4]], [[NAD-dependent hydrolysis|this mechanism]] is therefore distinct from the [[Glycoside_hydrolases#Mechanism|canonical Koshland mechanisms]] of glycoside hydrolysis. Notably, because oxidation occurs at C-3 of the sugar ring, followed by elimination at C-1, these enzymes can cleave both alpha- and beta-glycosides! Recently, [[User:Spencer Williams|Spencer]], [[User:Ethan Goddard-Borger|Ethan Goddard-Borger]], and [[User:Gideon Davies|Gideon Davies]] showed that [[NAD-dependent hydrolysis]] also extends to sulfoquinovoside hydrolysis by bacterial '''[[GH188]]''' members, complementing canonical sulfoquinovosidases in [[GH31]]. ''Read more about these remarkable enzymes '''[[GH188|here!]]'''''  
 
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'''16 June 2020:''' ''From rotting plants to vegetable digestion in the gut.'' The '''[[Polysaccharide Lyase Family 9]]''' page was completed by '''[[User:Ana Luis|Ana Luis]]''' and upgraded to [[Curator Approved]] status today by '''[[User:Wade Abbott|Wade Abbott]]'''.  '''[[PL9]]'''  was originally identified and characterized as part of the pectin-degrading machinery from the plant pathogenic bacterium [https://en.wikipedia.org/wiki/Dickeya_dadantii ''Dickeya dadantii''] (''Erwinia chrysanthemi''), including seminal structural work by [[User:Richard Pickersgill|Richard Pickersgill]] and colleagues. More recently '''[[User:Ana Luis|Ana]]''' and '''[[User:Wade Abbott|Wade]]''', as part of a big team involving other CAZypedians [[User:Jonathon Briggs|Jonathon Briggs]], [[User:Didier Ndeh|Didier Ndeh]], [[User:Alan Cartmell|Alan Cartmell]], [[User:Bernard Henrissat|Bernard Henrissat]], and [[User:Harry Gilbert|Harry Gilbert]], shed new light on the role of '''[[PL9]]''' members in the human gut microbiota. ''Take some time to learn more about the long and rich history of '''[[Polysaccharide Lyase Family 9]]!'''''
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'''16 August 2023:''' ''An oldie but a goodie.'' The page for '''[[CBM9]]''', one of the original founding top 10 [[Carbohydrate Binding Module Families]], has been completed by '''[[User:Johan Larsbrink|Johan Larsbrink]]''', who multitasked as both [[Author]] and [[Responsible Curator]]. '''[[CBM9]]''' members are often found in ultra-multimodular, xylan deconstructing, bacterial enzymes, and their cellulose-binding functionality has been exploited as affinity tags in recombinant protein purifications. ''Read more on this historically important [[Carbohydrate-binding modules|CBM]] family '''[[CBM9|here]]'''!''  
 
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Latest revision as of 19:00, 24 February 2024

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!


4 January 2024: CBM99, CBM100 and CBM101 in one fell swoop! Three new CBM families have been added to the CAZypedia repertoire. Though the families differ in their glycan targets, they share the interesting function of binding to highly complex sulfated marine polymers. Yaoguang Chang acted as Responsible Curator on all three pages. Xuanwei Mei authored the CBM99 and CBM101 red algal specific pages and Guanchen Liu authored the CBM100 glycosaminoglycan specific page. Learn more about CBM99, CBM100 and CBM101 on their respective pages!


4 January 2024: More "Fun" from the sea. Today, Yaoguang Chang Curator Approved the Glycoside Hydrolase Family 187 page Authored by Jingjing Shen. The founding member of GH187 is the alpha-1,3-L-fucanase ("Fun187A") the marine bacterium Wenyingzhuangia aestuarii, which recognizes a specific sulfated motif in sea cucumber fucans. GH187 is a small family (<50 members) and there remains much to elucidate regarding catalytic mechanism and enzyme structure. Interest in CAZymes active on marine biomass continues to grow, and we welcome this expansion in CAZypedia. Learn more about GH187 here!


17 December 2023: Redox-assisted glycoside hydrolysis, redux. Just before the turn of the new year, Spencer Williams completed the Glycoside Hydrolase Family 188 page. GH188 is the latest representative of a growing number of Glycoside Hydrolase families, including GH4, GH109, GH177, and GH179, which use an NAD-dependent oxidation-elimination-addition-reduction cycle to cleave glycosidic bonds. First established ca. 20 years ago in GH4, this mechanism is therefore distinct from the canonical Koshland mechanisms of glycoside hydrolysis. Notably, because oxidation occurs at C-3 of the sugar ring, followed by elimination at C-1, these enzymes can cleave both alpha- and beta-glycosides! Recently, Spencer, Ethan Goddard-Borger, and Gideon Davies showed that NAD-dependent hydrolysis also extends to sulfoquinovoside hydrolysis by bacterial GH188 members, complementing canonical sulfoquinovosidases in GH31. Read more about these remarkable enzymes here!


16 August 2023: An oldie but a goodie. The page for CBM9, one of the original founding top 10 Carbohydrate Binding Module Families, has been completed by Johan Larsbrink, who multitasked as both Author and Responsible Curator. CBM9 members are often found in ultra-multimodular, xylan deconstructing, bacterial enzymes, and their cellulose-binding functionality has been exploited as affinity tags in recombinant protein purifications. Read more on this historically important CBM family here!