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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'''16 November 2016:''' ''A new plant glycanase with a lysozyme fold:'' '''[[User:Spencer Williams|Spencer Williams]]''' does it again, with the completion of the '''[[Glycoside Hydrolase Family 134]]''' page on a new family of [[inverting]] beta-(gluco)mannanases.  This small family emerged in 2015 with the biochemical characterization of an ''Aspergillus nidulans'' (fungal) member. Recently the tertiary structure and detailed catalytic mechanism - including the reaction conformational itinerary - of a ''Streptomyces'' sp. '''[[Glycoside Hydrolase Family 134|GH134]]''' member has been resolved by [[User:Gideon Davies|Gideon Davies]], [[User:Spencer Williams|Spencer Williams]], and their collaborators and co-workers.  This is only the second example of a [[glycoside hydrolase]] family that utilizes a lysozyme-like fold as a scaffold for the cleavge of a plant polysaccharide, as opposed to bacterial peptidoglycan; the first, a [[Glycoside Hydrolase Family 124]] cellulase characterized by [[User:Harry Gilbert|Harry Gilbert]] ''et al.'', also uses an [[inverting]] mechanism.
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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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'''3 November 2016:''' ''New PDB links-out:'' For 3-D visualization of exemplar CAZymes and CBMs, we're trying a switch from [http://proteopedia.org/ Proteopedia] to the [https://doi.org/10.1093/nar/gkv402 NGL viewer] implementation at the RCSB Protein Data BankWe've made this switch site-wide across CAZypedia, and would like to [[Special:Contact|hear any feedback]] you might haveHere's an example for direct comparison: The seminal bacterial cellulose synthase complex [http://proteopedia.org/wiki/index.php/4hg6 in the JSMol viewer at Proteopedia] (including wiki page) and [http://www.rcsb.org/pdb/ngl/ngl.do?pdbid=4HG6 in the NGL viewer at the PDB] (other info available via the page tabs).
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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 2012Over 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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'''30 October 2016:''' ''Another X-module comes to light:'' Today '''[[User:Spencer Williams|Spencer Williams]]''' completed the '''[[Glycoside Hydrolase Family 135]]''' page, which describes the genesis of a new CAZy family from a small group of modules formerly known as "X307" in the [[User:Bernard Henrissat|CAZyModO]] classification. The single biochemically and structurally characterized GH135 member hydrolyzes the unique fungal exo-polysaccharide galactosaminogalactan, with crystallographic evidence suggesting that the enzyme acts as a alpha-galactosaminidase.  However, a number of key enzymological questions about this new family remain outstanding, and we look forward to future work in this direction of the CAZyme landscape.
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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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'''3 September 2016:''' ''Galactosaminoglycan degradation:'' '''[[User:Spencer Williams|Spencer Williams]]''' has just completed a short entry on '''[[Glycoside Hydrolase Family 114]]''', a small family of bacterial and fungal sequences currently represented by a single characterized endo-alpha-1,4-polygalactosaminidase.  alpha-1,4-Polygalactosamine, also known as galactosaminoglycan, is produced as a secreted polysaccharide by select fungi, including Aspergilli.
 
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'''27 February 2016:''' ''The sweet side of sulfur:'' [[Author]] '''[[User:Spencer Williams|Spencer Williams]]''' has updated the '''[[Glycoside Hydrolase Family 31]]''' page to reflect the recent discovery of the first dedicated sulfoquinovosidases (SQases), previously ‘hidden’ within this family. SQases cleave α-glycosides of sulfoquinovose (6-sulfoglucose), which represent a significant reservoir of organosulfur in the biosphere. ''See the [[GH31]] page to discover more of the hidden charms of this family.''
 
 
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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!