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| − | '''1 August 2019:''' ''Sweet Sixteen:'' The '''[[Carbohydrate Binding Module Family 16]]''' page in ''CAZypedia'' has been flipped to [[Curator Approved]] today. The page features '''[[CBM16]]''' members from two environmental bacteria with very different backgrounds: One bacterium was isolated from a red alga (red seaweed) and its [[GH16]] kappa-carrageenase-appended '''[[CBM16]]''' binds the red algal extracellular matrix polysaccharide carrageenan and influences the processive mechanism of the catalytic module. The other bacterium was isolated from organic waste leachate and deletion of both its [[CBM16]]s from a [[GH5]] mannanase severely impairs binding ability of the catalytic module. The '''[[CBM16]]''' page was [[Author]]ed by '''[[User:Maria Matard-Mann|Maria Matard-Mann]]''' with '''[[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]''' acting as [[Responsible Curator]]. ''Learn more about these "sweet sixteen" CBMs on the '''[[CBM16]]''' page.'' | + | '''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]]'''. |
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| − | '''21 July 2019:''' ''Back to the future:'' [[Author]] '''[[User:James Stevenson|James Stevenson]]''' and [[Responsible Curator]] '''[[User:Joel Weadge|Joel Weadge]]''' completed the '''[[Glycoside Hydrolase Family 105]]''' page today, which is related to the recently completed (see below) [[GH88]] page. Like [[GH88]], '''[[GH105]]''' comprises hexeuronic acid hydrolases that use a distinct mechanism of glycosidic bond cleavage. You can learn more about these enzymes on the '''[[GH105]]''' and [[GH88]] pages. ''We'd like to especially thank [[User:Joel Weadge|Joel]] and [[User:James Stevenson|James]] for taking the initiative to reach out on their own to offer to produce the [[GH105]] page; this is directly in the spirit of CAZypedia as a [http://dx.doi.org/10.1093/glycob/cwx089 community-led, volunteer resource!]'' | + | '''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.'' |
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| − | | + | '''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!'' |
| − | '''17 July 2019:''' ''A flashback on unsaturated glucuronyl hydrolases:'' Back in 2015, [[Author]] '''[[User:Seino Jongkees|Seino Jongkees]]''' essentially completed the '''[[Glycoside Hydrolase Family 88]]''' page, which was finally upgraded to [[Curator Approved]] status today. '''[[GH88]]''' unsaturated glucuronyl hydrolases use an atypical [[glycoside hydrolase]] mechanism that involves the hydration of the double bond between carbons 4 and 5 of the non-reducing terminal sugar of their substrates and subsequent rearrangement. In this way, the activity of '''[[GH88]]''' enzymes is dependent on the prior action of [[Polysaccharide Lyases]] to produce the required hexenuronic acid terminus. ''Learn more about these non-canonical enzymes, and their cousins in [[GH105]], on the '''[[GH88]]''' page''. | |
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| − | '''15 July 2019:''' ''Of carbohydrates, esters, and lignin:'' [[Author]]s '''[[User:Jenny Arnling Bååth|Jenny Arnling Bååth]]''' and '''[[User:Scott Mazurkewich|Scott Mazurkewich]]''', together with [[Responsible Curator]] '''[[User: Johan Larsbrink| Johan Larsbrink]]''' finalized ''CAZypedia's'' third [[Carbohydrate Esterase Families|Carbohydrate Esterase Family]] page today. '''[[Carbohydrate Esterase Family 15]]''' comprises glucuronoyl esterases that utilize a classical serine hydrolase catalytic triad to cleave pendant non-carbohydrate groups from, for example, plant glucuronoxylan (''i.e.'' [https://doi.org/10.1016/j.sbi.2005.10.008 de-esterification with the sugar as the acid]). '''[[CE15]]''' members have therefore be suggested to facilitate the breakdown of lignin-carbohydrate complexes (LCC) and are of growing interest for biomass processing. ''Learn more about these enzymes, including the seminal work of Peter Biely and colleagues, on the '''[[CE15]]''' page''.
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| − | '''5 June 2019:''' ''New and cool beta(1,2)-glucanases of GH162:'' Today [[Author]] '''[[User:Nobukiyo Tanaka|Nobukiyo Tanaka]]''' and [[Responsible Curator]] '''[[User:Masahiro Nakajima|Masahiro Nakajima]]''' completed the '''[[Glycoside Hydrolase Family 162]]''' page in ''CAZypedia''. As its high number would imply, '''[[GH162]]''' is one of the newest families in the CAZy classification, of which the first example has been elegantly characterized in 2019 by Drs. '''[[User:Nobukiyo Tanaka|Tanaka]]''' and '''[[User:Masahiro Nakajima|Nakajima]]''' and their colleagues. '''[[GH162]]''' is a tiny family of mostly fungal members, which has structural and mechanistic commonality with [[GH144]], and may be distantly related to [[GH8]] ([[Clan]] GH-M) and [[GH15]] ([[Clan]] GH-L). ''Learn more about all of these families on their respective pages''.
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| − | '''14 May 2019:''' ''Starch... it's not over yet:'' Two new families of starch-binding CBMs, '''[[CBM82]]''' and '''[[CBM83]]''', have joined the CAZypedia ranks. These CBMs are both found in an enormous multi-modular cell-wall anchored enzyme from a gut bacterium. The pages were both authored by '''[[User:Darrell Cockburn|Darrell Cockburn]]''' with '''[[User:Nicole Koropatkin|Nicole Koropatkin]]''' acting as responsible curator. ''Learn more about the new starch-binding '''[[CBM82]]''' and '''[[CBM83]]''' families on their respective pages''.
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| − | '''28 February 2019:''' ''CE9 is CE page #2!:'' Graduate student '''[[User:Alex Anderson|Alex Anderson]]''' has completed ''CAZypedia's'' second [[:Category:Carbohydrate Esterase Families|Carbohydrate Esterase (CE)]] family page, '''[[Carbohydrate Esterase Family 9]]''', which was [[Curator Approved]] by his supervisor '''[[User:Michael Suits|Michael Suits]]''' today. '''[[CE9]]''' enzymes are metal-dependent ''N''-acetylglucosamine 6-phosphate deacetylases that function in peptidoglycan recycling in bacteria. '''[[CE9]]''' is a huge family, currently comprising over 10,000 members (nearly all are from bacteria), which underscores their biological importance. '''[[User:Alex Anderson|Alex]]''' and '''[[User:Michael Suits|Mike]]''' completed ''CAZypedia's'' first [[:Category:Carbohydrate Esterase Families|CE family page]], [[CE4]] earlier this month, and we thank them for these seminal expansions of of our resource. ''Learn more about the structure and mechanism of metal-dependent deamidases here: [[CE9]], [[CE4]]''.
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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!