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Difference between revisions of "Glycoside Hydrolase Family 116"

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== Substrate specificities ==
 
== Substrate specificities ==
  
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 β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. 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.
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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 β-glucosidase GBA2, also known as glucocerebrosidase <cite>PMID17105727</cite>. 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.
  
  
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#PMID20427274 pmid=20427274
 
#PMID20427274 pmid=20427274
 
#PMID17105727 pmid=17105727
 
#PMID17105727 pmid=17105727
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#PMID15341727 pmid=15341727
 
</biblio>
 
</biblio>
  
  
 
[[Category:Glycoside Hydrolase Families|GH116]]
 
[[Category:Glycoside Hydrolase Families|GH116]]

Revision as of 02:39, 18 June 2010

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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 β-glucosidase GBA2, also known as glucocerebrosidase [2]. 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

The enzymes of this family are retaining glycoside hydrolases, and follow the classical Koshland double-displacement mechanism [3]. The stereochemistry of hydrolysis has been demonstrated by NMR using 4NP-b-Xyl as the substrate and S. solfataricus SSO1353 as the enzyme [1].


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 [4].
First catalytic nucleophile identification
Cite some reference here, with a short (1-2 sentence) explanation [5].
First general acid/base residue identification
Cite some reference here, with a short (1-2 sentence) explanation [6].
First 3-D structure
Cite some reference here, with a short (1-2 sentence) explanation [7].

References

  1. Cobucci-Ponzano B, Aurilia V, Riccio G, Henrissat B, Coutinho PM, Strazzulli A, Padula A, Corsaro MM, Pieretti G, Pocsfalvi G, Fiume I, Cannio R, Rossi M, and Moracci M. (2010). A new archaeal beta-glycosidase from Sulfolobus solfataricus: seeding a novel retaining beta-glycan-specific glycoside hydrolase family along with the human non-lysosomal glucosylceramidase GBA2. J Biol Chem. 2010;285(27):20691-703. DOI:10.1074/jbc.M109.086470 | PubMed ID:20427274 [PMID20427274]
  2. Boot RG, Verhoek M, Donker-Koopman W, Strijland A, van Marle J, Overkleeft HS, Wennekes T, and Aerts JM. (2007). Identification of the non-lysosomal glucosylceramidase as beta-glucosidase 2. J Biol Chem. 2007;282(2):1305-12. DOI:10.1074/jbc.M610544200 | PubMed ID:17105727 [PMID17105727]
  3. Rajan SS, Yang X, Collart F, Yip VL, Withers SG, Varrot A, Thompson J, Davies GJ, and Anderson WF. (2004). Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD+/Mn2+ -dependent phospho-alpha-glucosidase from Bacillus subtilis. Structure. 2004;12(9):1619-29. DOI:10.1016/j.str.2004.06.020 | PubMed ID:15341727 [PMID15341727]

All Medline abstracts: PubMed