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Difference between revisions of "Glycoside Hydrolase Family 91"

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* [[Responsible Curator]]: ^^^Bernard Henrissat^^^
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* Temporary [[Responsible Curator]]: ^^^Bernard Henrissat^^^
 
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=== GH91 is a deleted family ===
 
 
Entries in GH91 were transferred to [[Polysaccharide Lyase Family 19]] due to recommendations of the NC-IUBMB; polysaccharide cleavage occurs via intramolecular hydroxide attack, rather than glycosidic bond hydrolysis.
 
  
 
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{| {{Prettytable}}  
 
{| {{Prettytable}}  
 
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|{{Hl2}} colspan="2" align="center" |'''CAZy DB links'''
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|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH91'''
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|'''Clan'''   
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|'''Mechanism'''
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|'''Active site residues'''
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|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
 
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| colspan="2" |http://www.cazy.org/fam/GH91.html
 
| colspan="2" |http://www.cazy.org/fam/GH91.html
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| colspan="2" |http://www.cazy.org/fam/PL19.html
 
 
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== History of reclassification ==
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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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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>.
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== Substrate specificities ==
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Content is to be added here.
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== Kinetics and Mechanism ==
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Content is to be added here.
 +
 
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== Catalytic Residues ==
 +
Content is to be added here.
 +
 
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== Three-dimensional structures ==
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Content is to be added here.
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== Family Firsts ==
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;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 ==
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<biblio>
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#Sakurai1997 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. [http://dx.doi.org/10.1271/bbb.61.989 DOI: 10.1271/bbb.61.989]
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#Saito2003 pmid=16233453
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</biblio>
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[[Category:Glycoside Hydrolase Families|GH091]]
 
[[Category:Glycoside Hydrolase Families|GH091]]
[[Category:Deleted families]]
 

Revision as of 00:34, 20 April 2010

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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.


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 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 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

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
.
First catalytic nucleophile identification
.
First general acid/base residue identification
.
First 3-D structure
.

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]