CAZypedia needs your help! We have many unassigned GH, PL, CE, AA, GT, and CBM pages in need of Authors and Responsible Curators.
Scientists at all career stages, including students, are welcome to contribute to CAZypedia. Read more here, and in the 10th anniversary article in Glycobiology.
New to the CAZy classification? Read this first.
*
Consider attending the 15th Carbohydrate Bioengineering Meeting in Ghent, 5-8 May 2024.

Difference between revisions of "Glycoside Hydrolase Family 91"

From CAZypedia
Jump to navigation Jump to search
Line 1: Line 1:
* [[Responsible Curator]]: ^^^Bernard Henrissat^^^
+
<!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
 +
{{UnderConstruction}}
 +
* Temporary [[Responsible Curator]]: ^^^Bernard Henrissat^^^
 
----
 
----
 
=== 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.
 
  
 
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family -->
 
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family -->
 +
<div style="float:right">
 
{| {{Prettytable}}  
 
{| {{Prettytable}}  
 
|-
 
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB links'''
+
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH91'''
 +
|-
 +
|'''Clan'''   
 +
|
 +
|-
 +
|'''Mechanism'''
 +
|
 +
|-
 +
|'''Active site residues'''
 +
|
 +
|-
 +
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
 
|-
 
|-
 
| colspan="2" |http://www.cazy.org/fam/GH91.html
 
| colspan="2" |http://www.cazy.org/fam/GH91.html
|-
 
| colspan="2" |http://www.cazy.org/fam/PL19.html
 
 
|}
 
|}
 +
</div>
 
<!-- This is the end of the table -->
 
<!-- This is the end of the table -->
  
{{CuratorApproved}}
+
== 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]).
 +
 
 +
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>.
 +
 
 +
== 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 ==
 +
<biblio>
 +
#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]
 +
#Saito2003 pmid=16233453
 +
</biblio>
 +
 
 +
 
 
[[Category:Glycoside Hydrolase Families|GH091]]
 
[[Category:Glycoside Hydrolase Families|GH091]]
[[Category:Deleted families]]
 

Revision as of 01:34, 20 April 2010

Under construction icon-blue-48px.png

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]