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Difference between revisions of "Glycoside Hydrolase Family 116"
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== Substrate specificities == | == Substrate specificities == | ||
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This family of glycoside hydrolases was recently discovered characterising a new β-glucosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite>. This enzyme is distantly related to the human non-lysosomal bile acid b-glucosidase GBA2, also known as glucocerebrosidase. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) from the three domains of life. | This family of glycoside hydrolases was recently discovered characterising a new β-glucosidase from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' <cite>PMID20427274</cite>. This enzyme is distantly related to the human non-lysosomal bile acid b-glucosidase GBA2, also known as glucocerebrosidase. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) from the three domains of life. |
Revision as of 06:32, 17 June 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: ^^^Beatrice Cobucci-Ponzano^^^
- Responsible Curator: ^^^Marco Moracci^^^
Glycoside Hydrolase Family GH116 | |
Clan | GH-x |
Mechanism | retaining |
Active site residues | known |
CAZy DB link | |
https://www.cazy.org/GH116.html |
Substrate specificities
This family of glycoside hydrolases was recently discovered characterising a new β-glucosidase from the hyperthermophilic archaeon Sulfolobus solfataricus [1]. This enzyme is distantly related to the human non-lysosomal bile acid b-glucosidase GBA2, also known as glucocerebrosidase. GH116 contains acid β-glucosidase (EC 3.2.1.45), β-glucosidase (EC 3.2.1.21) and β-xylosidase (EC 3.2.1.37) from the three domains of life.
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 stereochemistry determination
- Cite some reference here, with a short (1-2 sentence) explanation [2].
- First catalytic nucleophile identification
- Cite some reference here, with a short (1-2 sentence) explanation [3].
- First general acid/base residue identification
- Cite some reference here, with a short (1-2 sentence) explanation [4].
- First 3-D structure
- Cite some reference here, with a short (1-2 sentence) explanation [5].
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 |
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Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006
- 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 |