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Difference between revisions of "Carbohydrate Esterase Family 6"
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| − | * [[Author]]: | + | * [[Author]]: [[User:Casper Wilkens|Casper Wilkens]] |
| − | * [[Responsible Curator]]: | + | * [[Responsible Curator]]: [[User:Harry Brumer|Harry Brumer]] |
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|- | |- | ||
|'''Fold''' | |'''Fold''' | ||
| − | | | + | |( α / β / α)-sandwich |
|- | |- | ||
|'''Mechanism''' | |'''Mechanism''' | ||
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== Substrate specificities == | == Substrate specificities == | ||
| − | Carbohydrate esterase family 6 (CE6) comprises only acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]) <cite>Cantarel2009</cite>. | + | Carbohydrate esterase family 6 (CE6) comprises only acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]) - an activity also found in families [[CE2]], [[CE3]], [[CE4]], [[CE5]], [[CE7]], and [[CE12]] <cite>Cantarel2009</cite>. |
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | + | CE6 acetyl xylan esterases target the 2-, 3- or 2,3-linked ''O''-acetyl substituents on the β-1,4-linked xylopyranosyl moieties that comprise the xylan backbone. | |
== Catalytic Residues == | == Catalytic Residues == | ||
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;First catalytic nucleophile identification: Content is to be added here. | ;First catalytic nucleophile identification: Content is to be added here. | ||
;First general acid/base residue identification: Content is to be added here. | ;First general acid/base residue identification: Content is to be added here. | ||
| − | ;First 3-D structure: | + | ;First 3-D structure: ''Arabidopsis thaliana apo'' acetyl xylan esterase in 2005 [https://www.rcsb.org/structure/2APJ PDB ID 2APJ] <cite>Bitto2005</cite>. |
== References == | == References == | ||
<biblio> | <biblio> | ||
| + | |||
#Cantarel2009 pmid=18838391 | #Cantarel2009 pmid=18838391 | ||
| + | |||
| + | #Bitto2005 pmid=16301800 | ||
| + | |||
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version]. | #DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version]. | ||
</biblio> | </biblio> | ||
[[Category:Carbohydrate Esterase Families|CE006]] | [[Category:Carbohydrate Esterase Families|CE006]] | ||
Latest revision as of 14:18, 18 December 2021
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 CE6 | |
| Fold | ( α / β / α)-sandwich |
| Mechanism | retaining/inverting |
| Active site residues | known/not known |
| CAZy DB link | |
| http://www.cazy.org/CE6.html | |
Substrate specificities
Carbohydrate esterase family 6 (CE6) comprises only acetylxylan esterases (EC 3.1.1.72) - an activity also found in families CE2, CE3, CE4, CE5, CE7, and CE12 [1].
Kinetics and Mechanism
CE6 acetyl xylan esterases target the 2-, 3- or 2,3-linked O-acetyl substituents on the β-1,4-linked xylopyranosyl moieties that comprise the xylan backbone.
Catalytic Residues
Content is to be added here.
Three-dimensional structures
Content is to be added here.
Family Firsts
- First stereochemistry determination
- Content is to be added here.
- First catalytic nucleophile identification
- Content is to be added here.
- First general acid/base residue identification
- Content is to be added here.
- First 3-D structure
- Arabidopsis thaliana apo acetyl xylan esterase in 2005 PDB ID 2APJ [2].
References
- Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 |
- Bitto E, Bingman CA, McCoy JG, Allard ST, Wesenberg GE, and Phillips GN Jr. (2005). The structure at 1.6 Angstroms resolution of the protein product of the At4g34215 gene from Arabidopsis thaliana. Acta Crystallogr D Biol Crystallogr. 2005;61(Pt 12):1655-61. DOI:10.1107/S0907444905034074 |
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Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. The Biochemist, vol. 30, no. 4., pp. 26-32. Download PDF version.