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Difference between revisions of "Glycoside Hydrolase Family 142"
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|'''Mechanism''' | |'''Mechanism''' | ||
| − | | | + | |not known |
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|'''Active site residues''' | |'''Active site residues''' | ||
| − | | | + | |not known |
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|{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | |{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | ||
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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'' < | + | The glycoside hydrolases from GH family 142 have β-L-arabinofuranosidase ([{{EClink}}3.2.1.185 EC 3.2.1.185]) activity. The first characterized enzyme from GH142 was the C-terminus of BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>. BT1020 C-terminus hydrolyses the β-1,5 linkage between L-arabinofuranosidase and D-DHA at the non-reducing end of rhamnogalacturonan II (RG II) D chain found in pectin. |
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
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== Catalytic Residues == | == Catalytic Residues == | ||
| − | The β-L-arabinofuranosidase from BT1020 C-terminus contains canonical glycoside hydrolase catalytic apparatus comprising carboxylate residues< | + | The β-L-arabinofuranosidase from BT1020 C-terminus contains canonical glycoside hydrolase catalytic apparatus comprising carboxylate residues <cite>Ndeh2017</cite>. |
== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | + | The β-L-arabinofuranosidase from the C-terminus of BT1020 has a (α/α)6-barrel structure <cite>Ndeh2017</cite>. | |
== Family Firsts == | == Family Firsts == | ||
| − | ;First stereochemistry determination: | + | ;First stereochemistry determination: Not yet identified. |
| − | ;First catalytic nucleophile identification: | + | ;First catalytic nucleophile identification: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>. |
| − | ;First general acid/base residue identification: | + | ;First general acid/base residue identification: Not yet identified. |
| − | ;First 3-D structure: | + | ;First 3-D structure: BT1020 from ''Bacteroides thetaiotaomicron'' <cite>Ndeh2017</cite>. |
== References == | == References == | ||
Latest revision as of 14:12, 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 | not known |
| Active site residues | 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 C-terminus hydrolyses the β-1,5 linkage between L-arabinofuranosidase and D-DHA at the non-reducing end 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 [1].
Three-dimensional structures
The β-L-arabinofuranosidase from the C-terminus of BT1020 has a (α/α)6-barrel structure [1].
Family Firsts
- First stereochemistry determination
- Not yet identified.
- First catalytic nucleophile identification
- BT1020 from Bacteroides thetaiotaomicron [1].
- First general acid/base residue identification
- Not yet identified.
- 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 |