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Carbohydrate Esterase Family 1

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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 1
Clan GH-x
Mechanism retaining/inverting
Active site residues known/not known
CAZy DB link
http://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] Ferulic acid esterases hydrolyze the ester bond linking the ferulic acid to the arabinose moiety, which decorate certain types of xylan.

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

  1. 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 | PubMed ID:24270786 [Lombard2014]
  2. 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 | PubMed ID:9162010 [Belisle1997]
  3. 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 | PubMed ID:10655617 [Ronning2000]
  4. 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 | PubMed ID:1409539 [Ollis1992]

All Medline abstracts: PubMed