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Carbohydrate Esterase Family 15

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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.


Carbohydrate Esterase Family CE15
Clan GH-x
Mechanism retaining/inverting
Active site residues known/not known
CAZy DB link
http://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