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Difference between revisions of "Glycoside Hydrolase Family 68"
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== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
− | Family GH68 enzymes are retaining enzymes, as first shown by Koshland and Stein by performing the reaction in | + | Family GH68 enzymes are retaining enzymes, as first shown by Koshland and Stein by performing the reaction in <sup>18</sup>O-labeled water and determining the <sup>18</sup>O content of the products <cite>1</cite>. |
− | |||
== Catalytic Residues == | == Catalytic Residues == | ||
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== Family Firsts == | == Family Firsts == | ||
− | ;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite> | + | ;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>1</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: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>. | ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>. |
Revision as of 03:45, 16 February 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: ^^^Tirso Pons^^^ and ^^^Wim Van den Ende^^^
- Responsible Curator: ^^^Wim Van den Ende^^^
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 [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 [5].
- First 3-D structure
- Cite some reference here, with a short (1-2 sentence) explanation [3].
References
You can even cite books using just the ISBN [6]. References that are not in PubMed can be typed in by hand [4].
- 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
- 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 |
- 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 |
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Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006