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Difference between revisions of "Glycoside Hydrolase Family 68"

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== Kinetics and Mechanism ==
 
== Kinetics and Mechanism ==
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Family GH68 enzymes are retaining enzymes, as first shown by Koshland and Stein by performing the reaction in 18O-labeled water and determining the 18O content of the products <cite>1</cite>.
  
  
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#1 pmid=13174523
 
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#X2 pmid=15869470
 
#X2 pmid=15869470

Revision as of 03:39, 16 February 2010

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Glycoside Hydrolase Family GH68
Clan GH-J
Mechanism retaining
Active site residues known
CAZy DB link
http://www.cazy.org/fam/GH68.html


Substrate specificities

Glycoside hydrolase family GH68 contains enzymes that hydrolyze fructose containing polysaccharides such as levansucrase (EC 2.4.1.10); β-fructofuranosidase (EC 3.2.1.26); and inulosucrase (EC 2.4.1.9)

Kinetics and Mechanism

Family GH68 enzymes are retaining enzymes, as first shown by Koshland and Stein by performing the reaction in 18O-labeled water and determining the 18O content of the products [1].


Catalytic Residues

Content is to be added here.


Three-dimensional structures

Currently, only two different three dimensional structures of family GH68 enzymes have been solved so far. The first crystal structure was reported for the bacterial levansucrase (SacB) from Bacillus subtilis subsp. subtilis str. 168 [2]. The second one corresponds to levansucrase (LdsA) from Gluconacetobacter diazotrophicus SRT4 [3].


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

You can even cite books using just the ISBN [7]. References that are not in PubMed can be typed in by hand [5].

  1. KOSHLAND DE Jr and STEIN SS. (1954). Correlation of bond breaking with enzyme specificity; cleavage point of invertase. J Biol Chem. 1954;208(1):139-48. | Google Books | Open Library PubMed ID:13174523 [1]
  2. Meng G and Fütterer K. (2003). Structural framework of fructosyl transfer in Bacillus subtilis levansucrase. Nat Struct Biol. 2003;10(11):935-41. DOI:10.1038/nsb974 | PubMed ID:14517548 [X1]
  3. Martínez-Fleites C, Ortíz-Lombardía M, Pons T, Tarbouriech N, Taylor EJ, Arrieta JG, Hernández L, and Davies GJ. (2005). Crystal structure of levansucrase from the Gram-negative bacterium Gluconacetobacter diazotrophicus. Biochem J. 2005;390(Pt 1):19-27. DOI:10.1042/BJ20050324 | PubMed ID:15869470 [X2]
  4. Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006

    [MikesClassic]
  5. Robert V. Stick and Spencer J. Williams. (2009) Carbohydrates. Elsevier Science. [3]

All Medline abstracts: PubMed