CAZypedia needs your help!
We have many unassigned pages in need of Authors and Responsible Curators. See a page that's out-of-date and just needs a touch-up? - You are also welcome to become a CAZypedian. Here's how.
Scientists at all career stages, including students, are welcome to contribute.
Learn more about CAZypedia's misson here and in this article.
Totally new to the CAZy classification? Read this first.

Difference between revisions of "Template:News"

From CAZypedia
Jump to navigation Jump to search
 
(205 intermediate revisions by 2 users not shown)
Line 1: Line 1:
'''1 August 2019:''' ''Sweet Sixteen:'' The [[CBM16]] CAZypedia page has been flipped to curator approved today.  It 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 moduleThe 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 authored 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 their [[CBM16]] CAZypedia page.
+
'''25 October 2024:''' ''Laminariawesome!'' Check out two new marine families of CBMs, '''[[CBM102]]''' and '''[[CBM103]]''', now on ''CAZypedia'' which have an ecological role in bacterial degradation of laminarin during phytoplankton bloomsSome function as surface glycan binding proteins but others have roles in targeting their appended catalytic modules to substrate. Both pages were [[author]]ed by '''[[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]'''. ''Read up on these environmentally important CBMs on their respective [[CBM102]] and [[CBM103]] pages!''
 
----
 
----
'''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!]''
+
'''19 July 2024:''' ''Chalk-up one more for the GTs!'' The '''[[Glycosyltransferase Family 47]]''' page joined the small group of [[Curator Approved]] [[Glycosyltransferase Families]] pages in ''CAZypedia'' today. This entry was [[author]]ed by Ph.D. students '''[[User:Daniel Tehrani|Daniel Tehrani]]''' and '''[[User:Charlie Corulli|Charlie Corulli]]''', and [[Responsible Curator|Curated]] by '''[[User:Breeanna Urbanowicz|Breeanna Urbanowicz]]''' with input from '''[https://ccrc.uga.edu/team/kelley-moremen/ Kelley Moremen]'''.  Widely represented in plants, '''[[GT47]]''' members are anomer-[[inverting]] [[glycosyltransferases]], which are involved in the biosynthesis of several cell wall matrix polysaccharides.  Representatives from mammals are involved in heparin biosynthesis.  Correspondingly, members of [[GH47]] have diverse substrate specificities, including the transfer of both anionic and neutral monosaccharides to polysaccharides.  ''This is a great example where two keen Ph.D. students worked with their supervisors to create a valuable page for the scientific community. We encourage others to follow their lead, on your favorite family!''
 
----
 
----
 +
'''9 July 2024:''' ''Yet another new family of beta-1,2-glucan-active enzymes!'' Today, '''[[User:Masahiro Nakajima|Masahiro Nakajima]]''' [[Curator Approved]] the '''[[Glycoside Hydrolase Family 186]]''' page by '''[[User:Sei Motouchi|Sei Motouchi]]'''. '''[[GH186]]''' is a family of anomer-[[inverting]] enzymes from bacteria, members of which are specific for beta-1,2-glucans.  Intriguingly, although some [[GH186]] members work as classic [[glycoside hydrolases]], others perform transglycosylation by wrapping the sugar chain around in the active-site, to position the 6-OH group of a terminal glucosyl unit for direct attack.  Also notable, [[GH186]] members appear to use an extended chain of water molecules to relay acceptor deprotonation by the [[general base]] residue, ''i.e.'' a [https://en.wikipedia.org/wiki/Grotthuss_mechanism Grotthuss mechanism]. ''Check out the '''[[GH186]]''' page to learn more about these interesting enzymes, and make sure to see the [[GH189]], [[GH144]], and [[GH162]] pages from this same group.''
  
'''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''.
 
 
----
 
----
'''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''.
+
'''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]]'''.  
 
 
----
 
'''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''.
 
----
 
'''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''.
 
----
 
'''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]]''.
 
 
----
 
----

Latest revision as of 05:59, 31 October 2024

25 October 2024: Laminariawesome! Check out two new marine families of CBMs, CBM102 and CBM103, now on CAZypedia which have an ecological role in bacterial degradation of laminarin during phytoplankton blooms. Some function as surface glycan binding proteins but others have roles in targeting their appended catalytic modules to substrate. Both pages were authored by Marie-Katherin Zühlke. Read up on these environmentally important CBMs on their respective CBM102 and CBM103 pages!


19 July 2024: Chalk-up one more for the GTs! The Glycosyltransferase Family 47 page joined the small group of Curator Approved Glycosyltransferase Families pages in CAZypedia today. This entry was authored by Ph.D. students Daniel Tehrani and Charlie Corulli, and Curated by Breeanna Urbanowicz with input from Kelley Moremen. Widely represented in plants, GT47 members are anomer-inverting glycosyltransferases, which are involved in the biosynthesis of several cell wall matrix polysaccharides. Representatives from mammals are involved in heparin biosynthesis. Correspondingly, members of GH47 have diverse substrate specificities, including the transfer of both anionic and neutral monosaccharides to polysaccharides. This is a great example where two keen Ph.D. students worked with their supervisors to create a valuable page for the scientific community. We encourage others to follow their lead, on your favorite family!


9 July 2024: Yet another new family of beta-1,2-glucan-active enzymes! Today, Masahiro Nakajima Curator Approved the Glycoside Hydrolase Family 186 page by Sei Motouchi. GH186 is a family of anomer-inverting enzymes from bacteria, members of which are specific for beta-1,2-glucans. Intriguingly, although some GH186 members work as classic glycoside hydrolases, others perform transglycosylation by wrapping the sugar chain around in the active-site, to position the 6-OH group of a terminal glucosyl unit for direct attack. Also notable, GH186 members appear to use an extended chain of water molecules to relay acceptor deprotonation by the general base residue, i.e. a Grotthuss mechanism. Check out the GH186 page to learn more about these interesting enzymes, and make sure to see the GH189, GH144, and GH162 pages from this same group.


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.