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Difference between revisions of "Carbohydrate Esterase Family 15"

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== Substrate specificities ==
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== Substrate specificity ==
Content is to be added here.
 
  
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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== Three-dimensional structures ==
 
 
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.
 
 
 
== Kinetics and Mechanism ==
 
Content is to be added here.
 
  
== Catalytic Residues ==
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== Catalytic Residues and Mechanism ==
Content is to be added here.
 
  
== Three-dimensional structures ==
 
Content is to be added here.
 
  
 
== Family Firsts ==
 
== Family Firsts ==
;First 3-D structure: The first solved structure of a CE15 enzyme was the Cip2 catalytic domain from Trichoderma reesei (TrGE) <cite>Pokkuluri2011</cite>.  
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;First 3-D structure: The first solved structure of a CE15 enzyme was the Cip2 catalytic domain from ''Trichoderma reesei'' (''Tr''GE) <cite>Pokkuluri2011</cite>.  
 
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;First mechanistic insight: The crystal structure of ''St''GE2 (from ''Sporotrichum thermophile'') in complex with the ligand 4-''O''-methyl-beta-D-glucopyranuronate gave the first direct insight into substrate binding <cite>Charavgi2013</cite>.
 
 
  
 
== References ==
 
== References ==
 
<biblio>
 
<biblio>
 
#Pokkuluri2011 pmid=21661060
 
#Pokkuluri2011 pmid=21661060
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#Charavgi2013 pmid=23275164
 
</biblio>
 
</biblio>
  
 
[[Category:Carbohydrate Esterase Families|CE015]]
 
[[Category:Carbohydrate Esterase Families|CE015]]

Revision as of 05:15, 28 January 2019

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Carbohydrate Esterase Family CE15
Clan GH-x
Mechanism retaining/inverting
Active site residues known/not known
CAZy DB link
https://www.cazy.org/CE15.html


Substrate specificity

Three-dimensional structures

Catalytic Residues and Mechanism

Family Firsts

First 3-D structure
The first solved structure of a CE15 enzyme was the Cip2 catalytic domain from Trichoderma reesei (TrGE) [1].
First mechanistic insight
The crystal structure of StGE2 (from Sporotrichum thermophile) in complex with the ligand 4-O-methyl-beta-D-glucopyranuronate gave the first direct insight into substrate binding [2].

References

  1. Pokkuluri PR, Duke NE, Wood SJ, Cotta MA, Li XL, Biely P, and Schiffer M. (2011). Structure of the catalytic domain of glucuronoyl esterase Cip2 from Hypocrea jecorina. Proteins. 2011;79(8):2588-92. DOI:10.1002/prot.23088 | PubMed ID:21661060 [Pokkuluri2011]
  2. Charavgi MD, Dimarogona M, Topakas E, Christakopoulos P, and Chrysina ED. (2013). The structure of a novel glucuronoyl esterase from Myceliophthora thermophila gives new insights into its role as a potential biocatalyst. Acta Crystallogr D Biol Crystallogr. 2013;69(Pt 1):63-73. DOI:10.1107/S0907444912042400 | PubMed ID:23275164 [Charavgi2013]

All Medline abstracts: PubMed