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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'''12 May 2011:''' ''A new page on a new-ish family:'' [[Author]] and [[Responsible Curator]] '''[[User:Satoshi Kaneko|Satoshi Kaneko]]''' completed the '''[[Glycoside Hydrolase Family 115]]''' page today.  '''[[GH115]]''' contains microbial alpha-glucuronidases, which are involved the cleavage of D-glucuronic acid and 4-O-methyl-D-glucuronic acid sidechains from xylans.  Remarkably, '''[[GH115]]''' enzymes can release these monosaccharides from intact polymer chains, which is rather rare for exo-acting enzymes, and contrasts them with glucuronidases from '''[[GH67]]'''.  Although this particular regiospecific activity has been known since the last millenium, it was only in 2009 that these particular enzymes nucleated their own GH 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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'''09 May 2011:''' ''It's a big news day here at CAZypedia.'' We are proud to announce that three distinct glycoside hydrolase family pages have been [[Curator Approved]] today:
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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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* '''[[Glycoside Hydrolase Family 74]]''' (written by '''[[User:Katsuro Yaoi|Katsuro Yaoi]]''' and '''[[User:Takuya Ishida|Takuya Ishida]]''', and curated by '''[[User:Katsuro Yaoi|Katsuro Yaoi]]''') is a family predominantly comprised of endo-glucanases that are specific for the plant polysaccharide xyloglucan (true xyloglucanases).
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* '''[[Glycoside Hydrolase Family 95]]''' (written and curated by '''[[User:Takane Katayama|Takane Katayama]]''') is a family of 1,2-α-L-fucosidases, members of which cleave human milk oligosaccharides, blood group glycoconjugates, and/or xyloglucan oligosaccharides.
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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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* '''[[Glycoside Hydrolase Family 117]]''' (written by '''[[User:Etienne Rebuffet|Etienne Rebuffet]]''' and curated by '''[[User:Mirjam Czjzek|Mirjam Czjzek]]''') is a small, newly created family of α-1,3-L-(3,6-anhydro)-galactosidases (neoagarobiose hydrolases), which catalyze the final step in the degradation of agars from red macroalgae in the marine environment.
 
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''We would like to express our sincere thanks to our Japanese and French colleagues for these important contributions to CAZypedia.''  Links to these families will be included in the next public update of the [http://www.cazy.org/ CAZy database] (expected soon!).
 
  
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''Special thanks also go to'' '''[[User:Etienne Rebuffet|Etienne]]''' ''for updating the'' '''[[Glycoside Hydrolase Family 82]]''' ''page,'' including a very cool animated image that highlights enzyme domain movement during substrate binding - CAZypedia really is a living resource that can be continually improved with the latest knowledge.
 
 
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'''28 April 2011:''' ''More on α-glucoside cleavage:'' [[Author]] and [[Responsible Curator]] '''[[User:Takashi Tonozuka|Takashi Tonozuka]]''' recently completed the '''[[Glycoside Hydrolase Family 63]]''' page, which has been updated to [[Curator Approved]] status today. '''[[GH63]]''' is especially notable as it contains the eukaryotic "processing α-glucosidase I enzymes," which are essential for N-glycan trimming during glycoprotein maturation.  '''[[User:Takashi Tonozuka|Takashi Tonozuka's]]''' group has done seminal structural elucidation work in this family, and we very much appreciate his contribution to ''CAZypedia'', especially during these tough times in Japan.
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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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'''21 March 2011:''' ''A new page on the equinox (as we thaw-out and welcome the sun back to the Baltic region):'' [[Responsible Curator]] '''[[User:Anna Kulminskaya|Anna Kulminskaya]]''' today approved the '''[[Glycoside Hydrolase Family 35]]''' page, which was written by '''[[User:Anna Kulminskaya|Anna]]''', with input on the 3-D structure section from '''[[User:Mirko Maksimainen|Mirko Maksimainen]]''' and '''[[User:Juha Rouvinen|Juha Rouvinen]]'''.  '''[[GH35]]''' is a family of &beta;-galactosidases from diverse organisms that display a range of bond specificities.  Only very few tertiary structures have been solved in this family, to which the Russian and Finnish groups have made seminal contributions.
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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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'''28 February 2011:''' ''Hexosaminidases!:'' The '''[[Glycoside Hydrolase Family 20]]''' and '''[[Glycoside Hydrolase Family 84]]''' pages, which were completed last week by [[Author]] '''[[User:Ian Greig|Ian Greig]]''' and approved by [[Responsible Curator]] '''[[User:David Vocadlo|David Vocadlo]]''', have today been cross-linked from the [http://www.cazy.org CAZy database] ''(look out for the next public release)''.  [[GH20]] is of significant medical relevance, as it contains the human enzymes HexA and HexB, deficiencies of which case Tay-Sachs disease and Sandhoff diseases, respectively.  [[GH84]] is similarly important in the context of cell and organism biology, as this family contains human OGA (HexC, MGEA5, ''O''-GlcNAcase), a nuclear and cytoplasmic enzyme that is responsible for dynamic modulation of β-linked ''O''-GlcNAc residues linked to serine and threonine residues. ''O''-GlcNAc'ylation of specific protein residues has in some cases been found to be reciprocal to phosphorylation and, accordingly, has implicated ''O''-GlcNAc in diverse cellular processes and disease states.
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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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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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