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'''28 April 2011:''' ''More on α-glucoside cleavage:'' [[Author]] and [[Responsible Curator]] '''[[User:Takashi Tonozuka|Takashi Tonozuka]]''' recently completed the '''[[Glycoside Hydrolase Family 63]]''' page, which has been updated to [[Curator Approved]] status today. '''[[GH63]]''' is especially notable as it contains the eukaryotic "processing α-glucosidase I enzymes," which are essential for N-glycan trimming during glycoprotein maturation. '''[[User:Takashi Tonozuka|Takashi Tonozuka's]]''' group has done seminal structural elucidation work in this family, and we very much appreciate his contribution to ''CAZypedia''.
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'''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 [[author]]ed by '''[[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]'''. ''Read up on these environmentally important CBMs on their respective [[CBM102]] and [[CBM103]] pages!''  
 
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'''21 March 2011:''' ''A new page on the equinox (as we thaw-out and welcome the sun back to the Baltic region):'' [[Responsible Curator]] '''[[User:Anna Kulminskaya|Anna Kulminskaya]]''' today approved the '''[[Glycoside Hydrolase Family 35]]''' page, which was written by '''[[User:Anna Kulminskaya|Anna]]''', with input on the 3-D structure section from '''[[User:Mirko Maksimainen|Mirko Maksimainen]]''' and '''[[User:Juha Rouvinen|Juha Rouvinen]]'''.  '''[[GH35]]''' is a family of β-galactosidases from diverse organisms that display a range of bond specificitiesOnly very few tertiary structures have been solved in this family, to which the Russian and Finnish groups have made seminal contributions.
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'''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!''
 
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'''28 February 2011:''' ''Hexosaminidases!:'' The '''[[Glycoside Hydrolase Family 20]]''' and '''[[Glycoside Hydrolase Family 84]]''' pages, which were completed last week by [[Author]] '''[[User:Ian Greig|Ian Greig]]''' and approved by [[Responsible Curator]] '''[[User:David Vocadlo|David Vocadlo]]''', have today been cross-linked from the [http://www.cazy.org CAZy database] ''(look out for the next public release)''.  [[GH20]] is of significant medical relevance, as it contains the human enzymes HexA and HexB, deficiencies of which case Tay-Sachs disease and Sandhoff diseases, respectively.  [[GH84]] is similarly important in the context of cell and organism biology, as this family contains human OGA (HexC, MGEA5, ''O''-GlcNAcase), a nuclear and cytoplasmic enzyme that is responsible for dynamic modulation of β-linked ''O''-GlcNAc residues linked to serine and threonine residues. ''O''-GlcNAc'ylation of specific protein residues has in some cases been found to be reciprocal to phosphorylation and, accordingly, has implicated ''O''-GlcNAc in diverse cellular processes and disease states.
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'''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-glucansIntriguingly, 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 attackAlso 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.''
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'''07 February 2011:''' ''A landmark CAZypedia page:'' This one has been a long time coming, but today '''[[User:Birte Svensson|Birte Svensson]]''' and '''[[User:Stefan Janecek|Stefan Janecek]]''' completed the '''[[Glycoside Hydrolase Family 13]]''' page.  '''[[GH13]]''' is, quite simply, THE family of α-glucoside-degrading and -rearranging enzymes, with over 10000 members distributed into more than 35 subfamilies, which represent tens of enzyme activities.  Due to the central role starch (amylose/amylopectin) and glycogen play in energy storage, these enzymes are of immense [http://dx.doi.org/10.1093/jxb/erq411 ecological] and [http://dx.doi.org/10.1016/S0168-1656(01)00407-2 biotechnological] importance. ''[[GH13]] is also our 70th [[Glycoside Hydrolase Families|Curator Approved GH Family]] page!!!''
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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]]'''.
 
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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.