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 See a page that's out-of-date and just needs a touch-up?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"
Harry Brumer (talk | contribs) |
Harry Brumer (talk | contribs) |
||
| Line 1: | Line 1: | ||
| + | '''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]]!'' | ||
| + | ---- | ||
'''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]. | ||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
---- | ---- | ||
Revision as of 02:01, 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.