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Difference between revisions of "Glycoside Hydrolase Family 20"
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== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
History of neighbouring group participation in enzyme-catalyzed REF Lowe and Sinnott and aqueous REF Sinnott and Bruice reactions of glycosides. Use of free energy relationships ships to infer neighbouring group participation. Early japanese work;REF Vocadlo and Withers differential analysis. REF | History of neighbouring group participation in enzyme-catalyzed REF Lowe and Sinnott and aqueous REF Sinnott and Bruice reactions of glycosides. Use of free energy relationships ships to infer neighbouring group participation. Early japanese work;REF Vocadlo and Withers differential analysis. REF | ||
| − | + | Loss of activity upon non-reducing end deacatylation <cite>Armand1997</cite>. | |
== Catalytic Residues == | == Catalytic Residues == | ||
| Line 49: | Line 49: | ||
;First sterochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>. | ;First sterochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>. | ||
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>MikesClassic</cite>. | ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>MikesClassic</cite>. | ||
| − | ;First general acid/base residue identification: | + | ;First general acid/base residue identification: Identified from the 3-D structure <cite>Tews1996</cite> and by analogy with closely related GH18 chitinases. |
| − | ;First 3-D structure: | + | ;First 3-D structure: The 3-D structure of the ''Serratia marscescens'' chitobiase <cite>Tews1996</cite>. |
== References == | == References == | ||
| Line 58: | Line 58: | ||
#3 isbn=978-0-240-52118-3 | #3 isbn=978-0-240-52118-3 | ||
#MikesClassic Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006] | #MikesClassic Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006] | ||
| − | + | #Armand1997 pmid=9396742 | |
| + | #Tews1996 pmid=8673609 | ||
</biblio> | </biblio> | ||
[[Category:Glycoside Hydrolase Families|GH020]] | [[Category:Glycoside Hydrolase Families|GH020]] | ||
Revision as of 09:40, 7 October 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: ^^^Ian Greig^^^
- Responsible Curator: ^^^David Vocadlo^^^
| Glycoside Hydrolase Family GH20 | |
| Clan | GH-K |
| Mechanism | retaining |
| Active site residues | known |
| CAZy DB link | |
| http://www.cazy.org/fam/GH20.html | |
Substrate specificities
Content is to be added here.
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
History of neighbouring group participation in enzyme-catalyzed REF Lowe and Sinnott and aqueous REF Sinnott and Bruice reactions of glycosides. Use of free energy relationships ships to infer neighbouring group participation. Early japanese work;REF Vocadlo and Withers differential analysis. REF Loss of activity upon non-reducing end deacatylation [5].
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
- Identified from the 3-D structure [6] and by analogy with closely related GH18 chitinases.
- First 3-D structure
- The 3-D structure of the Serratia marscescens chitobiase [6].
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 |
-
Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006
- Drouillard S, Armand S, Davies GJ, Vorgias CE, and Henrissat B. (1997). Serratia marcescens chitobiase is a retaining glycosidase utilizing substrate acetamido group participation. Biochem J. 1997;328 ( Pt 3)(Pt 3):945-9. DOI:10.1042/bj3280945 |
- Tews I, Perrakis A, Oppenheim A, Dauter Z, Wilson KS, and Vorgias CE. (1996). Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease. Nat Struct Biol. 1996;3(7):638-48. DOI:10.1038/nsb0796-638 |