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Difference between revisions of "Glycoside Hydrolase Family 17"
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== Substrate specificities == | == Substrate specificities == | ||
− | + | Normal 0 21 false false false FR X-NONE X-NONE MicrosoftInternetExplorer4 The family 17 glycoside hydrolases are clan GH-A enzymes from bacteria, fungi and plants, and include two major groups of enzymes with related but distinct substrate specificities, namely (1,3)-β-d-glucan endohydrolases (EC 3.1.2.39) and (1,3;1,4)-β-d-glucan endohydrolases (EC 3.1.2.73). A (1,3)-β-d-glucan exohydrolase (EC 3.1.2.58) is also classified in this family. The family 17 enzymes have quite distinct amino acid sequences and 3D structures compared with the (1,3)-β-d-glucan endohydrolases and (1,3;1,4)-β-d-glucan endohydrolases that have similar substrate specificities but are classified in families 16, 55, 64 and 81. | |
This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>3</cite>. References that are not in PubMed can be typed in by hand <cite>MikesClassic</cite>. | This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>3</cite>. References that are not in PubMed can be typed in by hand <cite>MikesClassic</cite>. |
Revision as of 12:58, 23 April 2010
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.
- Author: ^^^Geoff Fincher^^^
- Responsible Curator: ^^^Geoff Fincher^^^
Glycoside Hydrolase Family GHnn | |
Clan | GH-x |
Mechanism | retaining/inverting |
Active site residues | known/not known |
CAZy DB link | |
http://www.cazy.org/fam/GHnn.html |
Substrate specificities
Normal 0 21 false false false FR X-NONE X-NONE MicrosoftInternetExplorer4 The family 17 glycoside hydrolases are clan GH-A enzymes from bacteria, fungi and plants, and include two major groups of enzymes with related but distinct substrate specificities, namely (1,3)-β-d-glucan endohydrolases (EC 3.1.2.39) and (1,3;1,4)-β-d-glucan endohydrolases (EC 3.1.2.73). A (1,3)-β-d-glucan exohydrolase (EC 3.1.2.58) is also classified in this family. The family 17 enzymes have quite distinct amino acid sequences and 3D structures compared with the (1,3)-β-d-glucan endohydrolases and (1,3;1,4)-β-d-glucan endohydrolases that have similar substrate specificities but are classified in families 16, 55, 64 and 81.
This is an example of how to make references to a journal article [1]. (See the References section below). Multiple references can go in the same place like this [1, 2]. You can even cite books using just the ISBN [3]. References that are not in PubMed can be typed in by hand [4].
Kinetics and Mechanism
Content is to be added here.
Catalytic Residues
Content is to be added here.
Three-dimensional structures
Content is to be added here.
Family Firsts
- First sterochemistry determination
- Cite some reference here, with a short (1-2 sentence) explanation [1].
- First catalytic nucleophile identification
- Cite some reference here, with a short (1-2 sentence) explanation [4].
- First general acid/base residue identification
- Cite some reference here, with a short (1-2 sentence) explanation [2].
- First 3-D structure
- Cite some reference here, with a short (1-2 sentence) explanation [3].
References
- Comfort DA, Bobrov KS, Ivanen DR, Shabalin KA, Harris JM, Kulminskaya AA, Brumer H, and Kelly RM. (2007). Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases. Biochemistry. 2007;46(11):3319-30. DOI:10.1021/bi061521n |
- He S and Withers SG. (1997). Assignment of sweet almond beta-glucosidase as a family 1 glycosidase and identification of its active site nucleophile. J Biol Chem. 1997;272(40):24864-7. DOI:10.1074/jbc.272.40.24864 |
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Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006