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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]], [[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.'' | + | '''31 October 2025:''' ''A spooktacular addition to the CAZypedia family!'' Come and say 'Boo!' to the frighteningly well written '''[[CBM13]]''' ''CAZypedia'' page. The '''[[CBM13]]''' family is a '''[[Carbohydrate-binding_modules#Blurred Lines: CBMs, Lectins and Outliers|lectin-like CBM family]]'''. Its first characterized members were lectins, including the B chain from the highly toxic [https://en.wikipedia.org/wiki/Ricin ricin] toxin from ''Ricinus communis''. This spine tingling read was authored by '''[[User:Scott Mazurkewich|Scott Mazurkewich]]''' and '''[[User:Lauren McKee|Lauren McKee]]''' who also acted as responsible curator. ''Come and visit the scariest of ''CAZypedia'' CBM pages, '''[[CBM13|here!]]'''... if you dare...'' |
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| − | | + | '''29 July 2025:''' ''[[CBM91]] is in the news!'' The xylan binding '''[[CBM91]]''' family ''CAZypedia'' page is up and running. Appended to mainly [[GH43]] xylanases this [[CBM91]] family drives interaction with substrate. The [[CBM91]] page was authored by '''[[User:Daichi Ito|Daichi Ito]]''' who also discovered the initial xylan-binding function which resulted in the creation of the [[CBM91]] CAZy family. ''Read up on this industrially interesting '''[[CBM91]]''' family '''[[CBM91|here]]'''.'' |
| − | '''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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| − | '''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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| − | '''17 December 2023:''' ''Redox-assisted glycoside hydrolysis.'' 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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| − | '''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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31 October 2025: A spooktacular addition to the CAZypedia family! Come and say 'Boo!' to the frighteningly well written CBM13 CAZypedia page. The CBM13 family is a lectin-like CBM family. Its first characterized members were lectins, including the B chain from the highly toxic ricin toxin from Ricinus communis. This spine tingling read was authored by Scott Mazurkewich and Lauren McKee who also acted as responsible curator. Come and visit the scariest of CAZypedia CBM pages, here!... if you dare...
29 July 2025: CBM91 is in the news! The xylan binding CBM91 family CAZypedia page is up and running. Appended to mainly GH43 xylanases this CBM91 family drives interaction with substrate. The CBM91 page was authored by Daichi Ito who also discovered the initial xylan-binding function which resulted in the creation of the CBM91 CAZy family. Read up on this industrially interesting CBM91 family here.