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Difference between revisions of "Template:News"

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'''10 April 2017:''' ''A classic GH family:'' The '''[[Glycoside Hydrolase Family 22]]''' page was completed today by '''[[User:Spencer Williams|Spencer Williams]]''', with editorial input from '''[[User:David Vocadlo|David Vocadlo]]'''.  '''[[GH22]]''' contains the classic bacterial peptidoglycan hydrolase, hen egg-white lysozyme (HEWL), the first enzyme for which the three-dimensional structure was solved (reported in 1965).  Moreover, seminal enzyme-carbohydrate complex structures have made HEWL a paradigm for glycosidases that operate through the [[classical Koshland retaining mechanism]].  Although the nature of the glycosyl-enzyme intermediate remained contentious for many years since the original proposal of an oxacarbenium ion-carboxylate pair, a definitive study by  [[User:David Vocadlo|Vocadlo]], [[User:Gideon Davies|Davies]], Laine, and [[User:Steve Withers|Withers]] resolved the covalent nature of the glycosyl-enzyme HEWL, thus bring mechanistic understanding of this classic enzyme in concordance with other [[retaining]] GH families.  The lysozyme fold of HEWL defines the archtype for other hexosaminidases (i.e. those of [[GH19]] and [[GH23]]), and notably has also been observed in recently emergent families of cellulases ([[GH124]]) and mannanases ([[GH134]]).  ''Find out more about this classic GH family  [[Glycoside Hydrolase Family 22|here]]!''
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'''2 December 2016:''' ''A new CAZyme-specific journal:''  The journal ''[https://www.degruyter.com/view/j/amylase Amylase]'' has been recently launched under the editorial leadership of [[User:Stefan Janecek|Stefan Janecek]] and a number of other CAZypedians, including [[User:Bernard Henrissat|Bernard Henrissat]], [[User:Magali Remaud-Simeon|Magali Remaud-Simeon]], [[User:Birte Svensson|Birte Svensson]], [[User:Pedro Coutinho|Pedro Coutinho]], and [[User:Leila LoLeggio|Leila LoLeggio]].  ''[https://www.degruyter.com/view/j/amylase Amylase]'' is an open access journal that will focus on the biochemistry and biotechnology of starch hydrolases and related alpha-glucan-active enzymes, such as those from '''[[GH13]]''', '''[[GH70]]''', and '''[[GH77]]''' ([[Clan]] GH-H), as well as '''[[GH57]]''', '''[[GH119]]''', '''[[GH14]]''', '''[[GH15]]''', and '''[[GH31]]'''.  Visit the ''[https://www.degruyter.com/view/j/amylase Amylase]'' homepage for more information on the scope of the journal and details on how to [http://www.editorialmanager.com/amylase/ submit manuscripts for publication].
 
'''2 December 2016:''' ''A new CAZyme-specific journal:''  The journal ''[https://www.degruyter.com/view/j/amylase Amylase]'' has been recently launched under the editorial leadership of [[User:Stefan Janecek|Stefan Janecek]] and a number of other CAZypedians, including [[User:Bernard Henrissat|Bernard Henrissat]], [[User:Magali Remaud-Simeon|Magali Remaud-Simeon]], [[User:Birte Svensson|Birte Svensson]], [[User:Pedro Coutinho|Pedro Coutinho]], and [[User:Leila LoLeggio|Leila LoLeggio]].  ''[https://www.degruyter.com/view/j/amylase Amylase]'' is an open access journal that will focus on the biochemistry and biotechnology of starch hydrolases and related alpha-glucan-active enzymes, such as those from '''[[GH13]]''', '''[[GH70]]''', and '''[[GH77]]''' ([[Clan]] GH-H), as well as '''[[GH57]]''', '''[[GH119]]''', '''[[GH14]]''', '''[[GH15]]''', and '''[[GH31]]'''.  Visit the ''[https://www.degruyter.com/view/j/amylase Amylase]'' homepage for more information on the scope of the journal and details on how to [http://www.editorialmanager.com/amylase/ submit manuscripts for publication].
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'''29 November 2016:''' ''A small family of beta-xylosidases:''  The '''[[Glycoside Hydrolase Family 120]]''' page was completed and given [[Curator Approved]] status today by '''[[User:Spencer Williams|Spencer Williams]]'''.  '''[[Glycoside Hydrolase Family 120|GH120]]''' is currently a very small family, comprised of ca. 100 members originating exclusively from bacteria.  Following the initial identification of this family in 2011, enzymological and structural studies of two beta-xylosidases have revealed specifics of the catalytic mechanism ([[retaining]]) and an unusual beta-helix/beta-sandwich two-domain, tetrameric protein architecture.  Notably, the beta-helix domain resembles that of [[Polysaccharide Lyase Family 1]] and [[Glycoside Hydrolase Family 28]] members, and a complex structure with xylose revealed a large number of potential [[Surface Binding Site]]s.
 
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'''16 November 2016:''' ''A new plant glycanase with a lysozyme fold:'' '''[[User:Spencer Williams|Spencer Williams]]''' does it again, with the completion of the '''[[Glycoside Hydrolase Family 134]]''' page on a new family of [[inverting]] beta-(gluco)mannanases.  This small family emerged in 2015 with the biochemical characterization of an ''Aspergillus nidulans'' (fungal) member.  Recently the tertiary structure and detailed catalytic mechanism - including the reaction [[conformational itinerary]] - of a ''Streptomyces'' sp. (bacterial) '''[[Glycoside Hydrolase Family 134|GH134]]''' member has been resolved by [[User:Gideon Davies|Gideon Davies]], [[User:Spencer Williams|Spencer Williams]], and their collaborators and co-workers.  This is only the second example of a [[glycoside hydrolase]] family that utilizes a lysozyme-like fold as a scaffold for the cleavge of a plant polysaccharide, as opposed to bacterial peptidoglycan; the first, a [[Glycoside Hydrolase Family 124]] cellulase characterized by [[User:Harry Gilbert|Harry Gilbert]] ''et al.'', also uses an [[inverting]] mechanism.
 
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'''3 November 2016:''' ''New PDB links-out:'' For 3-D visualization of exemplar CAZymes and CBMs, we're trying a switch from [http://proteopedia.org/ Proteopedia] to the [https://doi.org/10.1093/nar/gkv402 NGL viewer] implementation at the RCSB Protein Data Bank.  We've made this switch site-wide across CAZypedia, and would like to [[Special:Contact|hear any feedback]] you might have.  Here's an example for direct comparison: The seminal bacterial cellulose synthase complex [http://proteopedia.org/wiki/index.php/4hg6 in the JSMol viewer at Proteopedia] (including wiki page) and [http://www.rcsb.org/pdb/ngl/ngl.do?pdbid=4HG6 in the NGL viewer at the PDB] (other info available via the page tabs).
 
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'''30 October 2016:''' ''Another X-module comes to light:'' Today '''[[User:Spencer Williams|Spencer Williams]]''' completed the '''[[Glycoside Hydrolase Family 135]]''' page, which describes the genesis of a new CAZy family from a small group of modules formerly known as "X307" in the [[User:Bernard Henrissat|CAZyModO]] classification. The single biochemically and structurally characterized GH135 member hydrolyzes the unique fungal exo-polysaccharide galactosaminogalactan, with crystallographic evidence suggesting that the enzyme acts as a alpha-galactosaminidase.  However, a number of key enzymological questions about this new family remain outstanding, and we look forward to future work in this direction of the CAZyme landscape.
 
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'''3 September 2016:''' ''Galactosaminoglycan degradation:'' '''[[User:Spencer Williams|Spencer Williams]]''' has just completed a short entry on '''[[Glycoside Hydrolase Family 114]]''', a small family of bacterial and fungal sequences currently represented by a single characterized endo-alpha-1,4-polygalactosaminidase.  alpha-1,4-Polygalactosamine, also known as galactosaminoglycan, is produced as a secreted polysaccharide by select fungi, including Aspergilli.
 
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'''27 February 2016:''' ''The sweet side of sulfur:'' [[Author]] '''[[User:Spencer Williams|Spencer Williams]]''' has updated the '''[[Glycoside Hydrolase Family 31]]''' page to reflect the recent discovery of the first dedicated sulfoquinovosidases (SQases), previously ‘hidden’ within this family. SQases cleave α-glycosides of sulfoquinovose (6-sulfoglucose), which represent a significant reservoir of organosulfur in the biosphere. ''See the [[GH31]] page to discover more of the hidden charms of this family.''
 
 
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Revision as of 03:01, 25 April 2017

10 April 2017: A classic GH family: The Glycoside Hydrolase Family 22 page was completed today by Spencer Williams, with editorial input from David Vocadlo. GH22 contains the classic bacterial peptidoglycan hydrolase, hen egg-white lysozyme (HEWL), the first enzyme for which the three-dimensional structure was solved (reported in 1965). Moreover, seminal enzyme-carbohydrate complex structures have made HEWL a paradigm for glycosidases that operate through the classical Koshland retaining mechanism. Although the nature of the glycosyl-enzyme intermediate remained contentious for many years since the original proposal of an oxacarbenium ion-carboxylate pair, a definitive study by Vocadlo, Davies, Laine, and Withers resolved the covalent nature of the glycosyl-enzyme HEWL, thus bring mechanistic understanding of this classic enzyme in concordance with other retaining GH families. The lysozyme fold of HEWL defines the archtype for other hexosaminidases (i.e. those of GH19 and GH23), and notably has also been observed in recently emergent families of cellulases (GH124) and mannanases (GH134). Find out more about this classic GH family here!

2 December 2016: A new CAZyme-specific journal: The journal Amylase has been recently launched under the editorial leadership of Stefan Janecek and a number of other CAZypedians, including Bernard Henrissat, Magali Remaud-Simeon, Birte Svensson, Pedro Coutinho, and Leila LoLeggio. Amylase is an open access journal that will focus on the biochemistry and biotechnology of starch hydrolases and related alpha-glucan-active enzymes, such as those from GH13, GH70, and GH77 (Clan GH-H), as well as GH57, GH119, GH14, GH15, and GH31. Visit the Amylase homepage for more information on the scope of the journal and details on how to submit manuscripts for publication.

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