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Difference between revisions of "Glycoside Hydrolase Family 142"
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== Substrate specificities == | == Substrate specificities == | ||
| − | + | The glycoside hydrolases from GH family 142 have β-L-arabinofuranosidase (EC 3.2.1.185) activity. The first characterized enzyme from GH142 was the C-terminus of BT1020 from ''Bacteroides thetaiotaomicron'' <ref>Ndeh2017</ref>. BT1020 hydrolyses the β-1,5 linkage between L-arabinofuranosidase and D-DHA in the terminal region of rhamnogalacturonan II (RG II) D chain found in pectin. | |
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== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | + | The kinetics and mechanisms of GH142 family remain to be elucidated. | |
== Catalytic Residues == | == Catalytic Residues == | ||
| − | + | The β-L-arabinofuranosidase from BT1020 C-terminus contains canonical glycoside hydrolase catalytic apparatus comprising carboxylate residues<ref>Ndeh2017</ref>. | |
== Three-dimensional structures == | == Three-dimensional structures == | ||
Revision as of 11:37, 25 August 2023
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 GH142 | |
| Clan | GH-x |
| Mechanism | retaining/inverting |
| Active site residues | known/not known |
| CAZy DB link | |
| https://www.cazy.org/GH142.html | |
Substrate specificities
The glycoside hydrolases from GH family 142 have β-L-arabinofuranosidase (EC 3.2.1.185) activity. The first characterized enzyme from GH142 was the C-terminus of BT1020 from Bacteroides thetaiotaomicron [1]. BT1020 hydrolyses the β-1,5 linkage between L-arabinofuranosidase and D-DHA in the terminal region of rhamnogalacturonan II (RG II) D chain found in pectin.
Kinetics and Mechanism
The kinetics and mechanisms of GH142 family remain to be elucidated.
Catalytic Residues
The β-L-arabinofuranosidase from BT1020 C-terminus contains canonical glycoside hydrolase catalytic apparatus comprising carboxylate residues[2].
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
- Content is to be added here.
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 |