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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Welcome to CAZypedia!
The Living Encyclopedia of Carbohydrate-Active Enzymes.
Cazypedia logo big.png

Purpose

CAZypedia has been initiated as a community-driven resource to assemble a comprehensive encyclopedia of the "CAZymes," the carbohydrate-active enzymes and associated carbohydrate-binding modules involved in the synthesis and degradation of complex carbohydrates. CAZypedia is inspired by, and closely connected with, the actively curated CAZy Database. It's probably fair to say that CAZypedians are, like our friends at the CAZy DB, a group of "biocurators."
If you are new to the CAZyme classification, "Sorting the Diverse" by Professors Gideon Davies and Michael Sinnott (The Biochemist, 2008, vol. 30, part 4, pp. 26-32) provides an excellent introduction and historical perspective.

Content

CAZypedia initially focussed on the Glycoside Hydrolase Families defined in the CAZy Database, and we continue to strive for complete coverage of this diverse class of enzymes. Other catabolic and anabolic CAZymes, as well as Auxiliary redox enzymes and non-catalytic Carbohydrate Binding Modules, continue to be incorporated as interest and engagement from the scientific community grows. In addition, there is a Lexicon of terms relevant to CAZymes and carbohydrate chemistry.
These and other aspects of CAZypedia's content can be accessed through the menus on the left side of each page.

How CAZypedia works

CAZypedia is built on authoring and editing principles similar to those of other expert-based online encyclopedias (cf. Citizendium, Scholarpedia). All contributors to CAZypedia, from the Authors to the Board of Curators, are experts in the field. Transparency is achieved through the use of contributors' real names and published biographies in CAZypedia. Individual entries in CAZypedia are managed by Responsible Curators, who are responsible for selecting expert Authors and coordinating author contributions on individual pages. Selection of Responsible Curators, based on their specialist expertise and ability to participate in the active maintenance of entry content, is handled by the Senior Curators.
More information on CAZypedia's content and editorial policies is available here.
A short lecture and a set of slides presenting CAZypedia are freely available here.
An article describing CAZypedia's genesis and evolution has been published in the journal Glycobiology.

Contact

If you would like to get involved with CAZypedia or suggest an improvement, please contact the Board of Curators.

Latest news

11 February 2024: A "BLAST" from the past, with a fresh update. Author Eduardo Moreno Prieto composed a new page on Glycoside Hydrolase Family 119,a family of bacterial amylases, which was Curator Approved by Stefan Janecek and Bernard Henrissat today. The first member of GH119 was characterized in 2006, and through sequence analysis with GH57 members, Janeček and Kuchtová predicted the active-site residues in 2012. Over a decade later, Eduardo, Bernard, and colleagues finally provided critical experimental support for these predictions. Learn more about this history, and especially the relationship between GH119 and GH57, in CAZypedia.

3 February 2024: A new family of beta-1,2-glucan-cyclizing enzymes. A page on the (currently) newest GH family, Glycoside Hydrolase Family 189, was completed today by Authors Tomoko Masaike, Masahiro Nakajima, and Nobukiyo Tanaka (Masahiro Nakajima is the Responsible Curator). GH189 is a family of bacterial transglycosylases that comprise a critical domain in cyclic beta-1,2-glucan synthase (CGS), because this domain is responsible for the final cyclization step during the biosynthesis of these key effector molecules. The discovery of GH189 builds on similarly exciting work by these authors and their colleagues on beta-1,2-glucan hydrolases in GH144 and GH162, which share a common protein fold with GH189, but have distinct mechansims. Check out the GH189, GH144, and GH162 pages to learn more about this breakthrough work on beta-1,2-glucan-active enzymes!


4 January 2024: CBM99, CBM100 and CBM101 in one fell swoop! Three new CBM families have been added to the CAZypedia repertoire. Though the families differ in their glycan targets, they share the interesting function of binding to highly complex sulfated marine polymers. Yaoguang Chang acted as Responsible Curator on all three pages. Xuanwei Mei authored the CBM99 and CBM101 red algal specific pages and Guanchen Liu authored the CBM100 glycosaminoglycan specific page. Learn more about CBM99, CBM100 and CBM101 on their respective pages!


4 January 2024: More "Fun" from the sea. Today, Yaoguang Chang Curator Approved the Glycoside Hydrolase Family 187 page Authored by Jingjing Shen. The founding member of GH187 is the alpha-1,3-L-fucanase ("Fun187A") the marine bacterium Wenyingzhuangia aestuarii, which recognizes a specific sulfated motif in sea cucumber fucans. GH187 is a small family (<50 members) and there remains much to elucidate regarding catalytic mechanism and enzyme structure. Interest in CAZymes active on marine biomass continues to grow, and we welcome this expansion in CAZypedia. Learn more about GH187 here!


17 December 2023: Redox-assisted glycoside hydrolysis, redux. Just before the turn of the new year, Spencer Williams completed the Glycoside Hydrolase Family 188 page. GH188 is the latest representative of a growing number of Glycoside Hydrolase families, including GH4, GH109, GH177, and GH179, which use an NAD-dependent oxidation-elimination-addition-reduction cycle to cleave glycosidic bonds. First established ca. 20 years ago in GH4, this mechanism is therefore distinct from the canonical Koshland mechanisms of glycoside hydrolysis. Notably, because oxidation occurs at C-3 of the sugar ring, followed by elimination at C-1, these enzymes can cleave both alpha- and beta-glycosides! Recently, Spencer, Ethan Goddard-Borger, and Gideon Davies showed that NAD-dependent hydrolysis also extends to sulfoquinovoside hydrolysis by bacterial GH188 members, complementing canonical sulfoquinovosidases in GH31. Read more about these remarkable enzymes here!


16 August 2023: An oldie but a goodie. The page for CBM9, one of the original founding top 10 Carbohydrate Binding Module Families, has been completed by Johan Larsbrink, who multitasked as both Author and Responsible Curator. CBM9 members are often found in ultra-multimodular, xylan deconstructing, bacterial enzymes, and their cellulose-binding functionality has been exploited as affinity tags in recombinant protein purifications. Read more on this historically important CBM family here!


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Dedication

CAZypedia is dedicated to the late Prof. Bruce Stone, whose enthusiasm to create a comprehensive encyclopedia of carbohydrate-active enzymes was essential in the genesis of this project.