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'''2 May 2013:''' ''Adding on to the Lexicon:'' Today '''[[User:Spencer Williams|Spencer Williams]]''' added the finishing touches to the [[Lexicon]] page on '''[[Transglycosylases]]'''.  Transglycosylation - the ability to ''non-hydrolytically'' rearrange glycosidic bonds between one or more substrates - is a feature of many [[Glycoside hydrolases]], especially those which use the [[retaining]] mechanism.  In such enzymes, the covalent glycosyl-enzyme reaction intermediate can be intercepted by either water (yielding hydrolysis) or a sugar "acceptor" substrate (yielding transglycosylation).  Although transglycosylation is generally a side activity of retaining enzymes, a handful are naturally very predominant '''[[Transglycosylases]]'''.  ''See the [[Lexicon]] page to learn more, including specific examples!''
 
'''2 May 2013:''' ''Adding on to the Lexicon:'' Today '''[[User:Spencer Williams|Spencer Williams]]''' added the finishing touches to the [[Lexicon]] page on '''[[Transglycosylases]]'''.  Transglycosylation - the ability to ''non-hydrolytically'' rearrange glycosidic bonds between one or more substrates - is a feature of many [[Glycoside hydrolases]], especially those which use the [[retaining]] mechanism.  In such enzymes, the covalent glycosyl-enzyme reaction intermediate can be intercepted by either water (yielding hydrolysis) or a sugar "acceptor" substrate (yielding transglycosylation).  Although transglycosylation is generally a side activity of retaining enzymes, a handful are naturally very predominant '''[[Transglycosylases]]'''.  ''See the [[Lexicon]] page to learn more, including specific examples!''
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'''16 Jan 2013:''' ''Class I mannosidases &times; Williams<sup>2</sup> = 90<sup>th</sup> CAZypedia GH page.'' '''[[User:Rohan Williams|Rohan Williams]]''' and '''[[User:Spencer Williams|Spencer Williams]]''' completed the '''[[Glycoside Hydrolase Family 47]]''' page today to give CAZypedia its 90<sup>th</sup> [[:Category:Curator approved|Curator Approved]] GH page.  '''[[GH47]]''' is particularly important because it contains alpha-1,2 mannosidases that are responsible for N-glycan processing in eukaryotes.  Delineated by subfamily membership, these eukaryotic mannosidases function either in glycoprotein maturation or endoplasmic reticulum-associated degradation (ERAD).  Very few bacterial '''[[GH47]]''' members are known, in contrast, and their function(s) has not been widely studied.  From a mechanistic perspective, '''[[GH47]]''' members are intriguing because the catalytic residues have not been unambiguously identified, despite high-resolution structure-function studies of these [[inverting]] enzymes.  ''Check out the [[GH47]] page to learn more!''
 
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'''14 Jan 2013:''' ''CAZypedia makes a contribution to MediaWiki community.'' We are proud to announce that [http://www.mediawiki.org/wiki/Extension:BiblioPlus BiblioPlus], an extension that provides automatic reference formatting to CAZypedia, has been officially accepted by the [http://www.mediawiki.org/wiki/Extension:BiblioPlus MediaWiki Extensions repository].  [http://www.mediawiki.org/wiki/Extension:BiblioPlus BiblioPlus] was coded by '''[[User:Karen Eddy|Karen Eddy]]''', a UBC computer science student working with '''[[User:Harry Brumer|Harry Brumer]]''', to resolve formatting issues with non-English characters in PubMed data.  [http://www.mediawiki.org/wiki/Extension:BiblioPlus BiblioPlus] is now available for anyone to use with any MediaWiki-based site to facilitate referencing journals and books. ''Thanks Karen, for all the hard work!''
 
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'''02 Dec 2012:''' ''Spencer does it again, twice.'' '''[[User:Spencer Williams|Spencer Williams]]''' has upgraded another two [[lexicon]] pages to [[:Category:Curator approved|Curator Approved]] status today.  Have no idea what '''[[Oxazolinium ion]]s''' and '''[[Oxocarbenium ion]]s''' are, or why they're important in [[glycosidase]]s?  ''Check out these new pages!''
 
 
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Revision as of 07:59, 17 May 2013

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2 May 2013: Adding on to the Lexicon: Today Spencer Williams added the finishing touches to the Lexicon page on Transglycosylases. Transglycosylation - the ability to non-hydrolytically rearrange glycosidic bonds between one or more substrates - is a feature of many Glycoside hydrolases, especially those which use the retaining mechanism. In such enzymes, the covalent glycosyl-enzyme reaction intermediate can be intercepted by either water (yielding hydrolysis) or a sugar "acceptor" substrate (yielding transglycosylation). Although transglycosylation is generally a side activity of retaining enzymes, a handful are naturally very predominant Transglycosylases. See the Lexicon page to learn more, including specific examples!