CAZypedia needs your help! We have many unassigned GH, PL, CE, AA, GT, and CBM pages in need of Authors and Responsible Curators.
Scientists at all career stages, including students, are welcome to contribute to CAZypedia. Read more here, and in the 10th anniversary article in Glycobiology.
New to the CAZy classification? Read this first.
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Consider attending the 15th Carbohydrate Bioengineering Meeting in Ghent, 5-8 May 2024.
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| − | '''21 March 2011:''' ''A new page on the equinox:'' [[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 specificities. Only very few tertiary structures have been solved in this family, to which the Russian and Finnish groups have made seminal contributions. | + | '''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 specificities. Only 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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'''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. | '''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. | ||
Revision as of 06:28, 22 March 2011
21 March 2011: A new page on the equinox (as we thaw-out and welcome the sun back to the Baltic region): Responsible Curator Anna Kulminskaya today approved the Glycoside Hydrolase Family 35 page, which was written by Anna, with input on the 3-D structure section from Mirko Maksimainen and Juha Rouvinen. GH35 is a family of β-galactosidases from diverse organisms that display a range of bond specificities. Only very few tertiary structures have been solved in this family, to which the Russian and Finnish groups have made seminal contributions.
28 February 2011: Hexosaminidases!: The Glycoside Hydrolase Family 20 and Glycoside Hydrolase Family 84 pages, which were completed last week by Author Ian Greig and approved by Responsible Curator David Vocadlo, have today been cross-linked from the 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.
07 February 2011: A landmark CAZypedia page: This one has been a long time coming, but today Birte Svensson and 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 ecological and biotechnological importance. GH13 is also our 70th Curator Approved GH Family page!!!