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Difference between revisions of "Glycoside Hydrolase Family 147"
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...") |
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|- | |- | ||
|'''Clan''' | |'''Clan''' | ||
| − | |GH- | + | |GH-A |
|- | |- | ||
|'''Mechanism''' | |'''Mechanism''' | ||
| − | |retaining | + | |retaining |
|- | |- | ||
|'''Active site residues''' | |'''Active site residues''' | ||
| − | | | + | |known |
|- | |- | ||
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | |{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | ||
| Line 29: | Line 29: | ||
== Substrate specificities == | == Substrate specificities == | ||
| − | + | The founding member of GH147, BACOVA_05493 a β1,4-galactosidase demonstrates a preference towards longer oligosaccharides releasing galacopyranose from the oligosaccharide chain. BACOVA_ is unable to hydrolyse galactobiose <cite>Luis2017</cite>. | |
| − | |||
| − | |||
| − | |||
| − | |||
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | + | NMR analysis of the hydrolysis product revealed a retaining mechanism of action <cite>Luis2017</cite>. | |
== Catalytic Residues == | == Catalytic Residues == | ||
| − | + | The catalytic nucleophile and general acid/base residues of the founding member of GH147, BACOVA_05493, were identified as Glu300 and Glu203, respectively <cite>Luis2017</cite>. | |
== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | + | Currently there is no crystal structure of any member of GH147. | |
== Family Firsts == | == Family Firsts == | ||
| − | ;First stereochemistry determination: | + | ;First stereochemistry determination: BACOVA_05493 from B. ovatus <cite>Luis2017</cite>. |
| − | ;First catalytic nucleophile identification: | + | ;First catalytic nucleophile identification: BACOVA_05493 from B. ovatus <cite>Luis2017</cite>. |
| − | ;First general acid/base residue identification: | + | ;First general acid/base residue identification: BACOVA_05493 from B. ovatus <cite>Luis2017</cite>. |
| − | ;First 3-D structure: | + | ;First 3-D structure: Currently not available. |
== References == | == References == | ||
<biblio> | <biblio> | ||
| − | # | + | #Luis2017 pmid=29255254 |
| − | |||
</biblio> | </biblio> | ||
[[Category:Glycoside Hydrolase Families|GH147]] | [[Category:Glycoside Hydrolase Families|GH147]] | ||
Revision as of 08:10, 18 January 2018
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.
- Author: ^^^Jonathon Briggs^^^
- Responsible Curator: ^^^Harry Gilbert^^^
| Glycoside Hydrolase Family GH147 | |
| Clan | GH-A |
| Mechanism | retaining |
| Active site residues | known |
| CAZy DB link | |
| http://www.cazy.org/GH147.html | |
Substrate specificities
The founding member of GH147, BACOVA_05493 a β1,4-galactosidase demonstrates a preference towards longer oligosaccharides releasing galacopyranose from the oligosaccharide chain. BACOVA_ is unable to hydrolyse galactobiose [1].
Kinetics and Mechanism
NMR analysis of the hydrolysis product revealed a retaining mechanism of action [1].
Catalytic Residues
The catalytic nucleophile and general acid/base residues of the founding member of GH147, BACOVA_05493, were identified as Glu300 and Glu203, respectively [1].
Three-dimensional structures
Currently there is no crystal structure of any member of GH147.
Family Firsts
- First stereochemistry determination
- BACOVA_05493 from B. ovatus [1].
- First catalytic nucleophile identification
- BACOVA_05493 from B. ovatus [1].
- First general acid/base residue identification
- BACOVA_05493 from B. ovatus [1].
- First 3-D structure
- Currently not available.
References
- Luis AS, Briggs J, Zhang X, Farnell B, Ndeh D, Labourel A, Baslé A, Cartmell A, Terrapon N, Stott K, Lowe EC, McLean R, Shearer K, Schückel J, Venditto I, Ralet MC, Henrissat B, Martens EC, Mosimann SC, Abbott DW, and Gilbert HJ. (2018). Dietary pectic glycans are degraded by coordinated enzyme pathways in human colonic Bacteroides. Nat Microbiol. 2018;3(2):210-219. DOI:10.1038/s41564-017-0079-1 |