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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 seaweed 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!]]''''' | + | '''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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| − | '''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!]]''''' | + | '''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]]'''.'' |
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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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| − | '''25 June 2023:''' ''Another one from the [https://en.wikipedia.org/wiki/Capybara capybara gut].'' We're pleased to announce that the '''[[Glycoside Hydrolase Family 173]]''' page, written by [[Author]]s '''[[User:Clelton Santos|Clelton Aparecido dos Santos]]''' and '''[[User:Gabriela Persinoti|Gabriela Felix Persinoti]]''' was [[Curator Approved]] by '''[[User:Mario Murakami|Mario Murakami]]''' today. This new family of beta-galactosidases was created through the same study of the capybara gut metagenome by the [[User:Mario Murakami|Murakami group]] that led to the creation of family [[CBM89]] (''see the June 22nd [[News]] item''). '''[[GH173]]''' appears to be distantly related to [[GH5]] and [[GH30]] in [[Clan]] GH-A, yet there remain many unknowns about this family and its founding member - ''read more [[GH173|here]]!''
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| − | '''23 June 2023:''' ''Human milk oligosaccharide metabolism.'' [[Author]] '''[[User:Chihaya Yamada|Chihaya Yamada]]''' and [[Responsible Curator]] '''[[User:Shinya Fushinobu|Shinya Fushinobu]]''' upgraded the '''[[Glycoside Hydrolase Family 136]]''' page to [[Curator Approved]] status today. '''[[GH136]]''' is a family of bacterial lacto-''N''-biosidases that release lacto-''N''-biose I and lactose from lacto-N-tetraose, the main component of human milk oligosaccharides. These enzymes have a comparatively rare right-handed beta helix fold that more typical of pectin-active [[PL]]s and [[GH]]s. ''Read more about these interesting enzymes and their role in the human gut microbiota [[GH136|here]]!''
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| − | '''22 June 2023:''' ''These [[CBM]]s are sizeable!'' The recently discovered xylan-binding '''[[CBM89]]''' family, originating from the capybara gut microbiota, is described by [[Author]]s '''[[User:Mariana Morais|Mariana Abrahão Bueno de Morais]]''' and '''[[User:Gabriela Persinoti|Gabriela Felix Persinoti]]'''. '''[[User:Mario Murakami|Mario Murakami]]''' acted as [[Responsible Curator]] on the [[CBM89|page]]. '''[[CBM89]]''' members are 600 - 1000 amino acids long which puts them in the upper echelons of CBM sizes - just as the capybara is to the rodent order. You can check out the write up on these unusually large CBMs on their '''[[CBM89]] ''[[CBM89|CAZypedia]]'' [[CBM89|page]]'''. | |
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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.