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Difference between revisions of "Polysaccharide Lyase Family 22"

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(Created page with " <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --> {{UnderConstruc...")
 
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<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
{{UnderConstruction}}
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{{CuratorApproved}}
* [[Author]]: ^^^Harry Brumer^^^
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* [[Author]]: ^^^Wade Abbott^^^
* [[Responsible Curator]]:  ^^^Harry Brumer^^^
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* [[Responsible Curator]]:  ^^^Wade Abbott^^^
 
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{| {{Prettytable}}  
 
{| {{Prettytable}}  
 
|-
 
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''
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|{{Hl2}} colspan="2" align="center" |'''Polysaccharide Lyase Family PL2'''
 
|-
 
|-
|'''Clan'''     
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|'''Mechanism'''     
|GH-x
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|&beta;-elimination
 
|-
 
|-
|'''Mechanism'''
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|'''Metal Cofactor'''
|retaining/inverting
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|manganese
 
|-
 
|-
 
|'''Active site residues'''
 
|'''Active site residues'''
|known/not known
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|known
 
|-
 
|-
 
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
 
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
 
|-
 
|-
| colspan="2" |{{CAZyDBlink}}GHnn.html
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| colspan="2" |{{CAZyDBlink}}PL22.html
 
|}
 
|}
 
</div>
 
</div>
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== Substrate specificities ==
 
== Substrate specificities ==
Content is to be added here.
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PL22 <cite>Abbott2010</cite>.  
  
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''
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== Kinetics and Mechanism ==
  
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.
 
  
== Kinetics and Mechanism ==
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== Catalytic Residues ==
Content is to be added here.
 
  
== Catalytic Residues ==
 
Content is to be added here.
 
  
 
== Three-dimensional structures ==
 
== Three-dimensional structures ==
Content is to be added here.
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== Family Firsts ==
 
== Family Firsts ==
;First stereochemistry determination: Content is to be added here.
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;First catalytic activity:
;First catalytic nucleophile identification: Content is to be added here.
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;First catalytic base identification:  
;First general acid/base residue identification: Content is to be added here.
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;First catalytic divalent cation identification:  
;First 3-D structure: Content is to be added here.
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;First 3-D structure:  
  
 
== References ==
 
== References ==
 
<biblio>
 
<biblio>
#Cantarel2009 pmid=18838391
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#Abbott2010 pmid=20851883
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]
 
 
</biblio>
 
</biblio>
  
[[Category:Glycoside Hydrolase Families|GHnnn]]
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[[Category:Polysaccharide Lyase Families|PL002]]
<!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. -->
 

Revision as of 06:48, 11 June 2014

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This page has been approved by the Responsible Curator as essentially complete. CAZypedia is a living document, so further improvement of this page is still possible. If you would like to suggest an addition or correction, please contact the page's Responsible Curator directly by e-mail.


Polysaccharide Lyase Family PL2
Mechanism β-elimination
Metal Cofactor manganese
Active site residues known
CAZy DB link
https://www.cazy.org/PL22.html


Substrate specificities

PL22 [1].

Kinetics and Mechanism

Catalytic Residues

Three-dimensional structures

Family Firsts

First catalytic activity
First catalytic base identification
First catalytic divalent cation identification
First 3-D structure

References

  1. Abbott DW, Gilbert HJ, and Boraston AB. (2010). The active site of oligogalacturonate lyase provides unique insights into cytoplasmic oligogalacturonate beta-elimination. J Biol Chem. 2010;285(50):39029-38. DOI:10.1074/jbc.M110.153981 | PubMed ID:20851883 [Abbott2010]