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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'''15 May 2020:''' ''A CBM20 for 2020!'' The multifunctional starch-disrupting, starch-binding and enzyme targeting [[CBM20]] family is now up and running in CAZypedia.  These pervasive CBMs have been identified in CAZy families including [[glycoside hydrolases]] and [[Auxiliary Activity Families|lytic polysaccharide monooxygenases]] but also in non-CAZy enzymes.  The page was authored by '''[[User:Marie Sofie Moeller|Marie Sofie Møller]]''' with '''[[User:Birte Svensson|Birte Svensson]]''' and '''[[User:Stefan Janecek|Stefan Janecek]]''' acting as responsible curators. ''Find out more on this starch-interacting [[CBM20]] family '''[[CBM20|here]]'''.''
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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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'''15 May 2020:''' ''More on beta(1,3)-glucanases.'' The '''[[Glycoside Hydrolase Family 64]]''' page, [[Author]]ed by '''[[User:Julie Grondin|Julie Grondin]]''', was completed and [[Curator Approved]] today. '''[[GH64]]''' comprises a group of β-1,3-glucanases, primarily from bacteria.The archetype of this family was originally cloned from a ''Streptomyces'' species in the late 1990's and was the subject of mechanistic and structural analysis through the first decade of the new millenium. Notably, analysis by a team led by '''[[User:Bernard Henrissat|Bernard Henrissat]]''' defined that this enzyme, and thus family, uses an [[inverting]] mechanism, further disntiguishing it from well-known [[retaining]] beta(1,3)-glucanases of [[GH16]], [[GH17]], and others, including the recently described [[GH158]] beta(1,3)-glucanases reported below. ''Read more about the unique '''[[Glycoside Hydrolase Family 64|Glycoside Hydrolase Family 64 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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'''11 May 2020:''' ''Three more from the gut.'' '''[[User:Alan Cartmell|Alan Cartmell]]''' completed no less than three new [[Glycoside Hydrolase Families|Glycoside Hydrolase Family]] pages on this day. '''[[Glycoside Hydrolase Family 137]]''', '''[[Glycoside Hydrolase Family 140]]''', and '''[[Glycoside Hydrolase Family 145]]''' were all created from a series of studies of Polysacchardie Utilization Loci from human gut bacteria by '''[[User:Harry Gilbert|Harry Gilbert]]'s''' group, to which '''[[User:Alan Cartmell|Alan]]''' contributed defining crystallography. '''[[User:Alan Cartmell|Alan]]''' has also taken over the duty of [[Responsible Curator]] of these pages following the retirement of the venerable '''[[User:Harry Gilbert|Professor Gilbert]]''', one of ''CAZypedia's'' [[CAZypedia:History|founding Senior Curators]].  ''Read more about the substrate specificity and structural biology of these three diverse families on their corresponding pages.''
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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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'''6 May 2020:''' ''CE #1!'' The first [[Carbohydrate Esterase Families|Carbohydrate Esterase Family]] page in the series, '''[[CE1]]''', was [[Curator Approved]] today.  [[Author]]ed by '''[[User:Casper Wilkens|Casper Wilkens]]''', the '''[[Carbohydrate Esterase Family 1]]''' page describes an old family of carbohydrate-specific and other esterases, members of which were identified through classical biochemistry before the present age of easy gene cloning and sequencing. Carbohydrate-active members of '''[[CE1]]''' include acetyl xylan esterases, cinnamoyl esterases, and feruloyl esterases responsible for hydrolyzing pendant acyl groups from plant cell wall matrix glycans (hemicelluloses). ''Read more about the long history of '''[[Carbohydrate Esterase Family 1]]''' here.''
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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 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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'''10 April 2020:''' ''Yet another new one from the gut.'' Today, [[Author]] '''[[User:Kazune Tamura|Kazune Tamura]]''' completed the '''[[Glycoside Hydrolase Family 158]]''' page. '''[[GH158]]''' emerged in 2019 from a high-throughput biochemical survey of sequences identified as distantly related to [[glycoside hydrolases]] by the CAZy team, who first demonstrated ''endo''-beta(1,3)-glucanase activity for the founding member of the family from the human gut bacterium ''Victivallis vadensis''. Contemporaneously, analysis of homolgos from human gut ''Bacteroides'' species by Guillaume Dejean and '''[[User:Kazune Tamura|Kazune Tamura]]''' resolved details of the specificity, mechanism, and tertiary structure of '''[[GH158]]''' members in Polysaccharide Utilization Loci. ''Read about the detailed history and juicy details of this new GH family '''[[Glycoside Hydrolase Family 158|here]]'''.''
 
 
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'''8 April 2020:''' ''Another new one from the gut.'' The '''[[Glycoside Hydrolase Family 164]]''' page, which was [[author]]ed by '''[[User:Zachary Armstrong|Zachary Armstrong]]''', was upgraded to [[Curator Approved]] status by [[Responsible Curator]] '''[[User:Gideon Davies|Gideon Davies]]''' today. '''[[Glycoside Hydrolase Family 164]]''' is yet another newly discovered [[Glycoside Hydrolase Families|GH family]] from a human gut bacterium - this time through a large-scale effort by teams at AFMB and CERMAV spearheaded by [[User:Bernard Henrissat|Bernard Henrissat]]. The founding member of '''[[GH164]]''' is a beta-mannosidase from ''Bacteroides salyersiae'', on which '''[[User:Zachary Armstrong|Zach]]''' and  '''[[User:Gideon Davies|Gideon]]''' performed a classic mechanistic and structural analysis to define the central aspects of catalysis in this new family. ''Read more about this new - and currently tiny - GH family '''[[Glycoside Hydrolase Family 164|here]]'''.''
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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!

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