CAZypedia needs your help!
We have many unassigned pages in need of Authors and Responsible Curators. See a page that's out-of-date and just needs a touch-up? - You are also welcome to become a CAZypedian. Here's how.
Scientists at all career stages, including students, are welcome to contribute.
Learn more about CAZypedia's misson here and in this article.
Totally new to the CAZy classification? Read this first.
Glycoside Hydrolase Family 143
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.
| Glycoside Hydrolase Family GH143 | |
| Clan | GH-x |
| Mechanism | retaining/inverting |
| Active site residues | known/not known |
| CAZy DB link | |
| https://www.cazy.org/GH143.html | |
Substrate specificities
The members of GH142 family are 1-keto-3-deoxy-D-lyxo-heptulosaric acid (DHA) hydrolases (EC 3.2.1.-). The first characterized enzyme from this family was the N-terminus of BT1020 from Bacteroides thetaiotaomicron [1]. BT1020 cleaves the D-DHA- β-2,3-D-GalA linkage in rhamnogalacturonan II (RG II) in pectin.
Kinetics and Mechanism
Content is to be added here.
Catalytic Residues
The active site of DHA-hydrolase (N-terminus of BT1020) contains tyrosine and glutamate residues that function as the catalytic nucleophile and acid-base residues [1].
Three-dimensional structures
The N-terminus of BT1020 is made of 380 amino acid residues, arranged into 5-bladed β-propeller structure with 2-keto-3-deoxy-D-lyxo-heptulosaric acid (DHA)-hydrolase activity [1].
Family Firsts
- First stereochemistry determination
- Not yet identified.
- First catalytic nucleophile identification
- BT1020 from Bacteroides thetaiotaomicron [1].
- First general acid/base residue identification
- BT1020 from Bacteroides thetaiotaomicron [1].
- First 3-D structure
- BT1020 from Bacteroides thetaiotaomicron [1].
References
- Ndeh D, Rogowski A, Cartmell A, Luis AS, Baslé A, Gray J, Venditto I, Briggs J, Zhang X, Labourel A, Terrapon N, Buffetto F, Nepogodiev S, Xiao Y, Field RA, Zhu Y, O'Neil MA, Urbanowicz BR, York WS, Davies GJ, Abbott DW, Ralet MC, Martens EC, Henrissat B, and Gilbert HJ. (2017). Complex pectin metabolism by gut bacteria reveals novel catalytic functions. Nature. 2017;544(7648):65-70. DOI:10.1038/nature21725 |