|
|
| (109 intermediate revisions by 2 users not shown) |
| Line 1: |
Line 1: |
| − | '''22 Spetember 2020:''' ''Like PLs, but different:'' We are happy to announce the completion of a new [[Lexicon]] page on [[Polysaccharide epimerases]] today. '''[[User:Margrethe Gaardlos|Margrethe Gaardlos]]''' spearheaded the composition of this new page, with input from co-[[author]] '''[[User:Anne Tondervik|Anne Tøndervik]]''' and [[Responsible Curator]] '''[[User:Finn Aachmann|Finn Lillelund Aachmann]]'''. Although they are not categorized into families in the CAZy system, [[Polysaccharide epimerases]] bear a lot of structural and mechanistic similarity to [[Polysaccharide Lyases]]: Instead of catalyzing an elimination reaction to break poly-uronic acid chains, [[Polysaccharide epimerases]] simply use the first part of the [[PL]] mechanism to remove and re-add the C-5 proton. The resulting change in the configuration of the C-6 carboxylate has major impacts on polysaccharide structure and properties. ''The Norwegian team has done a tremendous job in capturing the broad history of these enzymes, including their diverse substrate specificities and structures, which you can read all about [[Polysaccharide epimerases|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]]'''. |
| | ---- | | ---- |
| − | | + | '''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.'' |
| − | '''6 August 2020:''' ''A beta-1,3-glucanase family with a deep history:'' '''[[User:Julie Grondin|Julie Grondin's]]''' '''[[Glycoside Hydrolase Family 81]]''' page was [[Curator Approved]] by '''[[User:Al Boraston|Al Boraston]]''' today. '''[[GH81]]''' has a long history of discovery and mechanistic study, including by original CAZypedian and [https://www.grc.org/carbohydrate-active-enzymes-for-glycan-conversions-conference/default.aspx Cellulase/CAZyme GRC co-founder] '''[[User:David Wilson|David Wilson]]''' and co-workers. By capturing a phenomenal number of oligosaccharide complexes, '''[[User:Al Boraston|Al's]]''' group has recently provided detailed molecular description of how enzymes in this family specifically recognize the helical structure adopted by beta-1,3-glucans. ''Be sure to check out the [[Glycoside Hydrolase Family 81|GH81 page]] to get the full history of the contributions of a number of groups world-wide to our knowledge of this family.'' | |
| − | | |
| | ---- | | ---- |
| − | '''23 July 2020:''' ''Another CE family page from our friends at WLU!'' The '''[[Carbohydrate Esterase Family 7]]''' page was finalized and promoted to [[Curator Approved]] status today. '''[[User:Joel Weadge|Joel Weadge]]''' and '''[[User:Joel Weadge|Michael Suits]]''' have been leading the completion of a bunch of CE pages with the help of keen students from Wilfred Laurier University (see [[CE3]], [[CE4]], and [[CE9]]). This time, '''[[User:Emily Rodriguez|Emily Rodriguez]]''' produced the '''[[CE7]]''' page, which encompasses acetyl xylan esterases and cephalosporin-C deacetylases. ''Learn more about the specificity, mechanism, and three-dimensional structure of CE7 enzymes [[Carbohydrate Esterase Family 7|here]].'' | + | '''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!'' |
| − | | |
| − | ----
| |
| − | '''19 June 2020:''' ''Three additional alginate lyase families!'' The number of PL family pages in ''CAZypedia'' continues to grow with the promotion of the '''[[Polysaccharide Lyase Family 6]]''', '''[[Polysaccharide Lyase Family 15]]''', and '''[[Polysaccharide Lyase Family 17]]''' pages to [[Curator Approved]] status today. We thank '''[[User:Emil Stender|Emil G.P. Stender]]''' for his hard work in tackling this trifecta of bacterial alginate lyase families (including some heparin/heparan sulfate lyases from the human gut microbiota in '''[[PL15]]'''), which were vetted [[Responsible Curator]] '''[[User:Birte Svensson|Birte Svensson]]'''. ''Dig into the details of these families on the '''[[PL6]]''', '''[[PL15]]''', and '''[[PL17]]''' pages, in comparison with the recently completed '''[[PL7]]''' page (see previous news item, below).''
| |
| − | ----
| |
| − | '''17 June 2020:''' ''PLs from the sea.'' The '''[[Polysaccharide Lyase Family 7]]''' page, which was written by '''[[User:Nadine Gerlach|Nadine Gerlach]]''', was promoted to completed by [[Curator Approved]] status today by '''[[User:Jan-Hendrik Hehemann|Jan-Hendrik Hehemann]]'''. The founding member of '''[[PL7]]''', an alginate lyase, was characterized way back in 1993 by a team notably including CAZypedian [[User:Gurvan Michel|Gurvan Michel]]. Alginate is heteropolysaccharide from brown algae and mucoid bacteria, consisting of beta-{{Smallcaps|d}}-mannuronate (M) and alpha-{{Smallcaps|l}}-guluronate (G) residues in varying ratios and intra-chain distributions, depending on the source. As a result, '''[[PL7]]''' members exhibit mannuronate, guluronate, or mixed link specificity. ''Read more about the deep history of enzymolgoy and structural biology of PL7 [[Polysaccharide Lyase Family 7|here]], including seminal work by '''[[User:Jan-Hendrik Hehemann|Jan-Hendrik]]''' showing the horizontal gene transfer of these enzymes into the human gut microbiota and other marine bacteria.''
| |
| − | ----
| |
| − | '''16 June 2020:''' ''From rotting plants to vegetable digestion in the gut.'' The '''[[Polysaccharide Lyase Family 9]]''' page was completed by '''[[User:Ana Luis|Ana Luis]]''' and upgraded to [[Curator Approved]] status today by '''[[User:Wade Abbott|Wade Abbott]]'''. '''[[PL9]]''' was originally identified and characterized as part of the pectin-degrading machinery from the plant pathogenic bacterium [https://en.wikipedia.org/wiki/Dickeya_dadantii ''Dickeya dadantii''] (''Erwinia chrysanthemi''), including seminal structural work by [[User:Richard Pickersgill|Richard Pickersgill]] and colleagues. More recently '''[[User:Ana Luis|Ana]]''' and '''[[User:Wade Abbott|Wade]]''', as part of a big team involving other CAZypedians [[User:Jonathon Briggs|Jonathon Briggs]], [[User:Didier Ndeh|Didier Ndeh]], [[User:Alan Cartmell|Alan Cartmell]], [[User:Bernard Henrissat|Bernard Henrissat]], and [[User:Harry Gilbert|Harry Gilbert]], shed new light on the role of '''[[PL9]]''' members in the human gut microbiota. ''Take some time to learn more about the long and rich history of '''[[Polysaccharide Lyase Family 9]]!'''''
| |
| | ---- | | ---- |
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!