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 See a page that's out-of-date and just needs a touch-up?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.
Difference between revisions of "Glycoside Hydrolase Family 139"
Harry Brumer (talk | contribs) (Created page with "<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --> {{UnderConstruct...") |
Harry Brumer (talk | contribs) m (Text replacement - "\^\^\^(.*)\^\^\^" to "$1") |
||
| (7 intermediate revisions by 4 users not shown) | |||
| Line 1: | Line 1: | ||
| − | + | {{CuratorApproved}} | |
| − | + | * [[Author]]: [[User:Ana Luis|Ana Luis]] | |
| − | * [[Author]]: | + | * [[Responsible Curator]]: [[User:Harry Gilbert|Harry Gilbert]] |
| − | * [[Responsible Curator]]: | ||
---- | ---- | ||
| Line 12: | Line 11: | ||
|- | |- | ||
|'''Clan''' | |'''Clan''' | ||
| − | | | + | |none |
|- | |- | ||
|'''Mechanism''' | |'''Mechanism''' | ||
| − | | | + | |unknown |
|- | |- | ||
|'''Active site residues''' | |'''Active site residues''' | ||
| − | | | + | |not known |
|- | |- | ||
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | |{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | ||
| Line 29: | Line 28: | ||
== Substrate specificities == | == Substrate specificities == | ||
| − | + | [[Glycoside hydrolases]] of family 139 family display α-2-''O''-methyl-L-fucosidase activity. They are exclusively bacterial in origin. The enzyme BT0984 from ''Bacteroides thetaiotaomicron'' is the only member of this family that has been characterized. This ''exo''-acting enzyme targets the 2-''O''-methyl-L-fucose-α-1,2-D-Galp linkage in chain B of the complex pectin rhamnogalacturonan-II <cite>Ndeh2017</cite>. | |
| − | |||
| − | |||
| − | |||
| − | |||
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | + | The stereochemistry of the reaction catalyzed by GH139 members has not yet been reported. | |
== Catalytic Residues == | == Catalytic Residues == | ||
| − | + | Not known. | |
== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | + | No three-dimensional structure has been solved for this family. | |
== Family Firsts == | == Family Firsts == | ||
| − | ;First stereochemistry determination: | + | ;First stereochemistry determination: Unknown. |
| − | ;First catalytic nucleophile identification: | + | ;First catalytic nucleophile identification: Unknown. |
| − | ;First general acid/base residue identification: | + | ;First general acid/base residue identification: Unknown. |
| − | ;First 3-D structure: | + | ;First 3-D structure: Unknown. |
== References == | == References == | ||
<biblio> | <biblio> | ||
| − | # | + | #Ndeh2017 pmid=28329766 |
| − | |||
</biblio> | </biblio> | ||
[[Category:Glycoside Hydrolase Families|GH139]] | [[Category:Glycoside Hydrolase Families|GH139]] | ||
Latest revision as of 13:20, 18 December 2021
This page has been approved by the Responsible Curator as essentially complete. CAZypedia is a living document, so further improvement of this page is still possible. If you would like to suggest an addition or correction, please contact the page's Responsible Curator directly by e-mail.
| Glycoside Hydrolase Family GH139 | |
| Clan | none |
| Mechanism | unknown |
| Active site residues | not known |
| CAZy DB link | |
| https://www.cazy.org/GH139.html | |
Substrate specificities
Glycoside hydrolases of family 139 family display α-2-O-methyl-L-fucosidase activity. They are exclusively bacterial in origin. The enzyme BT0984 from Bacteroides thetaiotaomicron is the only member of this family that has been characterized. This exo-acting enzyme targets the 2-O-methyl-L-fucose-α-1,2-D-Galp linkage in chain B of the complex pectin rhamnogalacturonan-II [1].
Kinetics and Mechanism
The stereochemistry of the reaction catalyzed by GH139 members has not yet been reported.
Catalytic Residues
Not known.
Three-dimensional structures
No three-dimensional structure has been solved for this family.
Family Firsts
- First stereochemistry determination
- Unknown.
- First catalytic nucleophile identification
- Unknown.
- First general acid/base residue identification
- Unknown.
- First 3-D structure
- Unknown.
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 |