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"

From CAZypedia
Jump to navigation Jump to search
 
(272 intermediate revisions by 2 users not shown)
Line 1: Line 1:
−
'''10 September 2017:''' ''Sussing out starch recognition in CBM58:'' We are excited to report that '''[[User:Nicole Koropatkin|Nicole Koropatkin]]''' has completed the '''[[Carbohydrate Binding Module Family 58]]''' page today.  [[CBM58]] constitutes a comparatively small family of CBMs found in bacteria in the phylum Bacteroidetes, including key members of the human gut microbiota such as ''Bacteroides thetaiotaomicron''.  Within these bacteria, [[CBM58]] modules are found inserted within the [[GH13]] catalytic module of SusG, the essential outer-membrane-bound amylase of the starch utilization system (sus).  [[User:Nicole Koropatkin|Nicole’s]] seminal structural biology has defined the family and provided insight into the recognition of amylose helices by [[CBM58]] members in SusG homologs.  ''Read more about this fascinating system [[Carbohydrate Binding Module Family 58|here]].''    
+
'''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]]'''.
 
----
 
----
−
'''10 April 2017:''' ''A classic GH family:'' The '''[[Glycoside Hydrolase Family 22]]''' page was completed today by '''[[User:Spencer Williams|Spencer Williams]]''', with editorial input from [[Responsible Curator]] '''[[User:David Vocadlo|David Vocadlo]]'''.  '''[[GH22]]''' contains the classic bacterial peptidoglycan hydrolase, hen egg-white lysozyme (HEWL), the first enzyme for which the three-dimensional structure was solved (reported in 1965).  Moreover, seminal enzyme-carbohydrate complex structures have made HEWL a paradigm for glycosidases that operate through the [[classical Koshland retaining mechanism]].  Although the nature of the reaction intermediate remained contentious for many years since the original proposal of an oxacarbenium ion-carboxylate pair, a definitive study by [[User:David Vocadlo|Vocadlo]], [[User:Gideon Davies|Davies]], Laine, and [[User:Steve Withers|Withers]] resolved the covalent nature of the glycosyl-enzyme HEWL in 2001, thus bringing mechanistic understanding of this classic enzyme in concordance with other [[retaining]] GH families. The lysozyme fold of HEWL defines the archetype for other hexosaminidases (i.e. those of [[GH19]] and [[GH23]]) and the non-catalytic alpha-lactalbumins, and this fold notably has also been observed in recently emergent families of cellulases ([[GH124]]) and mannanases ([[GH134]]).  ''Find out more about this classic GH family  [[Glycoside Hydrolase Family 22|here]]!''
+
'''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.''
 +
----
 +
'''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!''
 
----
 
----

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!

Retrieved from "http://www.cazypedia.org/index.php?title=Template:News&oldid=18023"