CAZypedia needs your help!
We have many unassigned pages in need of Authors and Responsible Curators. See a page that's out-of-date needs a touch-up? - you are welcome to become a CAZypedian. Here's how.
Scientists at all career stages, including students, are welcome to contribute
Read more about CAZypedia here, and in the 10th anniversary article in Glycobiology.
New to the CAZy classification? Read this first.

Difference between revisions of "Template:News"

From CAZypedia
Jump to navigation Jump to search
 
(418 intermediate revisions by 3 users not shown)
Line 1: Line 1:
'''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'' growing [[lexicon]] of terms and concepts.
+
'''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]]'''.  
 
----
 
----
'''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) deconstructionThe '''[[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!
+
'''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 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.''
 
----
 
----
'''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]].
+
'''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!''
----
 
'''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]]!
 
 
----
 
----

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!