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Difference between revisions of "Carbohydrate Esterase Family 15"
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− | == Substrate | + | == Substrate specificity == |
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− | + | == Three-dimensional structures == | |
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− | == | ||
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− | == Catalytic Residues == | + | == Catalytic Residues and Mechanism == |
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== Family Firsts == | == Family Firsts == | ||
− | ;First 3-D structure: The first solved structure of a CE15 enzyme was the Cip2 catalytic domain from Trichoderma reesei ( | + | ;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>. |
− | + | ;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>. | |
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== References == | == References == | ||
<biblio> | <biblio> | ||
#Pokkuluri2011 pmid=21661060 | #Pokkuluri2011 pmid=21661060 | ||
+ | #Charavgi2013 pmid=23275164 | ||
</biblio> | </biblio> | ||
[[Category:Carbohydrate Esterase Families|CE015]] | [[Category:Carbohydrate Esterase Families|CE015]] |
Revision as of 05:15, 28 January 2019
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.
- Author: ^^^Jenny Arnling Bååth^^^ and ^^^Scott Mazurkewich^^^
- Responsible Curator: ^^^Johan Larsbrink^^^
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
- 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 |
- 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 |