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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]]''' ([[ | + | '''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 how to submit manuscripts for publication. |
| − | 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 how to 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. | '''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. | ||
Revision as of 11:07, 2 December 2016
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 how to submit manuscripts for publication.
29 November 2016: A small family of beta-xylosidases: The Glycoside Hydrolase Family 120 page was completed and given Curator Approved status today by Spencer Williams. 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 Sites.
16 November 2016: A new plant glycanase with a lysozyme fold: 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) GH134 member has been resolved by Gideon Davies, 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 Harry Gilbert et al., also uses an inverting mechanism.
3 November 2016: New PDB links-out: For 3-D visualization of exemplar CAZymes and CBMs, we're trying a switch from Proteopedia to the NGL viewer implementation at the RCSB Protein Data Bank. We've made this switch site-wide across CAZypedia, and would like to hear any feedback you might have. Here's an example for direct comparison: The seminal bacterial cellulose synthase complex in the JSMol viewer at Proteopedia (including wiki page) and in the NGL viewer at the PDB (other info available via the page tabs).
30 October 2016: Another X-module comes to light: Today 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 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.
3 September 2016: Galactosaminoglycan degradation: 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.
27 February 2016: The sweet side of sulfur: Author 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.