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Difference between revisions of "Glycoside Hydrolase Family 91"

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== History of reclassification ==
 
== History of reclassification ==
Entries in [[Glycoside Hydrolase Family 91]] were originally reclassified to [[Polysaccharide Lyase Family 19]] on 30 July 2008 due to recommendations of the NC-IUBMB, which stated that these enzymes are lyases, as there is no water involved in the reaction.  Indeed, polysaccharide cleavage in some members occurs via intramolecular hydroxide attack, rather than glycosidic bond hydrolysis (see EC [{{EClink}}4.2.2.17 4.2.2.17] and EC [{{EClink}}4.2.2.18 4.2.2.18]).
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Entries in [[Glycoside Hydrolase Family 91]] were reclassified to [[Polysaccharide Lyase Family 19]] on 30 July 2008 due to recommendations of the NC-IUBMB, which stated that these enzymes are lyases, as there is no water involved in the reaction.  Indeed, polysaccharide cleavage in some members occurs via intramolecular hydroxide attack, rather than glycosidic bond hydrolysis (see EC [{{EClink}}4.2.2.17 4.2.2.17] and EC [{{EClink}}4.2.2.18 4.2.2.18]).
  
 
The family was ''re-reclassified'' as [[Glycoside Hydrolase Family 91]] on 20 April 2010 due to direct analogy with the lytic transglycosidases of [[GH23]], [[GH102]], [[GH103]], and [[GH104]].  Additionally, a hydrolase (di-fructofuranose 1,2':2,3' dianhydride hydrolase, DFA-IIIase) has also been found in this family <cite>Sakurai1997 Saito2003</cite>.
 
The family was ''re-reclassified'' as [[Glycoside Hydrolase Family 91]] on 20 April 2010 due to direct analogy with the lytic transglycosidases of [[GH23]], [[GH102]], [[GH103]], and [[GH104]].  Additionally, a hydrolase (di-fructofuranose 1,2':2,3' dianhydride hydrolase, DFA-IIIase) has also been found in this family <cite>Sakurai1997 Saito2003</cite>.

Revision as of 01:47, 20 April 2010

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Glycoside Hydrolase Family GH91
Clan
Mechanism
Active site residues
CAZy DB link
http://www.cazy.org/fam/GH91.html

History of reclassification

Entries in Glycoside Hydrolase Family 91 were reclassified to Polysaccharide Lyase Family 19 on 30 July 2008 due to recommendations of the NC-IUBMB, which stated that these enzymes are lyases, as there is no water involved in the reaction. Indeed, polysaccharide cleavage in some members occurs via intramolecular hydroxide attack, rather than glycosidic bond hydrolysis (see EC 4.2.2.17 and EC 4.2.2.18).

The family was re-reclassified as Glycoside Hydrolase Family 91 on 20 April 2010 due to direct analogy with the lytic transglycosidases of GH23, GH102, GH103, and GH104. Additionally, a hydrolase (di-fructofuranose 1,2':2,3' dianhydride hydrolase, DFA-IIIase) has also been found in this family [1, 2].

Substrate specificities

Content is to be added here.

Kinetics and Mechanism

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Catalytic Residues

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Three-dimensional structures

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Family Firsts

First stereochemistry determination
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First catalytic nucleophile identification
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First general acid/base residue identification
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First 3-D structure
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References

  1. H. Sakurai, A. Yokota, Y. Sumita, Y. Mori, H. Matsui and F. Tomita, Metabolism of DFA III by Arthrobacter sp. H65-7: purification and properties of a DFA III hydrolysis enzyme (DFA IIIase). Biosci. Biotechnol. Biochem. 61 (1997), pp. 989–993. DOI: 10.1271/bbb.61.989

    [Sakurai1997]
  2. Saito K, Sumita Y, Nagasaka Y, Tomita F, and Yokota A. (2003). Molecular cloning of the gene encoding the di-D-Fructofuranose 1,2':2,3' dianhydride hydrolysis enzyme (DFA IIIase) from Arthrobacter sp. H65-7. J Biosci Bioeng. 2003;95(5):538-40. DOI:10.1016/s1389-1723(03)80058-0 | PubMed ID:16233453 [Saito2003]