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Difference between revisions of "Carbohydrate Esterase Family 1"
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== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
Content is to be added here. | Content is to be added here. | ||
| + | Mycolyltransferases transfer of the mycolyl group from α,α′-trehalose monomycolate to a second α,α′-trehalose monomycolate molecule forming α,α′-trehalose dimycolate <cite>Belisle1997</cite> | ||
== Catalytic Residues == | == Catalytic Residues == | ||
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#Lombard2014 pmid=24270786 | #Lombard2014 pmid=24270786 | ||
#Ronning2000 pmid=10655617 | #Ronning2000 pmid=10655617 | ||
| − | + | #Belisle1997 pmid=9162010 | |
| − | #Ollis1992 | + | #Ollis1992 pmid=1409539 |
</biblio> | </biblio> | ||
[[Category:Carbohydrate Esterase Families|CE001]] | [[Category:Carbohydrate Esterase Families|CE001]] | ||
Revision as of 05:54, 1 February 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: ^^^Casper Wilkens^^^
- Responsible Curator:
| Carbohydrate Esterase Family 1 | |
| Clan | GH-x |
| Mechanism | retaining/inverting |
| Active site residues | known/not known |
| CAZy DB link | |
| https://www.cazy.org/CE1.html | |
Substrate specificities
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC 3.1.1.72), feruloyl esterases (EC 3.1.1.73), cinnamoyl esterases (EC 3.1.1-), carboxylesterases (EC 3.1.1.1), S-formylglutathione hydrolases (EC 3.1.2.12), diacylglycerol O-acyltransferases (EC 2.3.1.20), and thehalose 6-O-mycolyltransferases (EC 2.3.1.122) and others [1].
Kinetics and Mechanism
Content is to be added here. Mycolyltransferases transfer of the mycolyl group from α,α′-trehalose monomycolate to a second α,α′-trehalose monomycolate molecule forming α,α′-trehalose dimycolate [2]
Catalytic Residues
Content is to be added here.
Three-dimensional structures
CE1's are members of the α/β-hydrolase superfamily [3], which are comprised of central β-strands connected by α-helices [4].
Family Firsts
- First characterized
- Content is to be added here.
- First mechanistic insight
- The crystal structure of Mycobacterium tuberculosis H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad [3].
- First 3-D structure
- Mycobacterium tuberculosis H37Rv mycolyltransferase crystal structure in 2000 [3].
References
- Lombard V, Golaconda Ramulu H, Drula E, Coutinho PM, and Henrissat B. (2014). The carbohydrate-active enzymes database (CAZy) in 2013. Nucleic Acids Res. 2014;42(Database issue):D490-5. DOI:10.1093/nar/gkt1178 |
- Belisle JT, Vissa VD, Sievert T, Takayama K, Brennan PJ, and Besra GS. (1997). Role of the major antigen of Mycobacterium tuberculosis in cell wall biogenesis. Science. 1997;276(5317):1420-2. DOI:10.1126/science.276.5317.1420 |
- Ronning DR, Klabunde T, Besra GS, Vissa VD, Belisle JT, and Sacchettini JC. (2000). Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines. Nat Struct Biol. 2000;7(2):141-6. DOI:10.1038/72413 |
- Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, and Schrag J. (1992). The alpha/beta hydrolase fold. Protein Eng. 1992;5(3):197-211. DOI:10.1093/protein/5.3.197 |