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Difference between revisions of "Glycoside Hydrolase Family 140"
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== Substrate specificities == | == Substrate specificities == | ||
| − | + | Thus far only one member of the family has been characterised, BT1012 from bacteroides thetaiotaomicron. BT1012 displays apiosidase activity targeting apiose in the complex glycan rhamnogalacturonan ii (RGII). The apiose is found at the base of Chains A and B in RGII and linked α1,2 to the galacturonic acid backbone. Cleavage of the backbone must occur for BT1012 to then act. | |
| − | |||
| − | |||
| − | |||
| − | |||
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | + | GH140 uses a, retaining, double displacement mechanism. This was shown by methanolysis and analysis of the methyl-apiose product was done by HPLC and mass spectrometry. | |
== Catalytic Residues == | == Catalytic Residues == | ||
| − | + | The catalytic residues are an aspartate and glutamate located on beta strands 4 and 7 respectively. | |
== Three-dimensional structures == | == Three-dimensional structures == | ||
Revision as of 12:40, 15 December 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: ^^^Alan Cartmell^^^
- Responsible Curator: ^^^Harry Gilbert^^^
| Glycoside Hydrolase Family GH140 | |
| Clan | GH-x |
| Mechanism | retaining |
| Active site residues | known |
| CAZy DB link | |
| https://www.cazy.org/GH140.html | |
Substrate specificities
Thus far only one member of the family has been characterised, BT1012 from bacteroides thetaiotaomicron. BT1012 displays apiosidase activity targeting apiose in the complex glycan rhamnogalacturonan ii (RGII). The apiose is found at the base of Chains A and B in RGII and linked α1,2 to the galacturonic acid backbone. Cleavage of the backbone must occur for BT1012 to then act.
Kinetics and Mechanism
GH140 uses a, retaining, double displacement mechanism. This was shown by methanolysis and analysis of the methyl-apiose product was done by HPLC and mass spectrometry.
Catalytic Residues
The catalytic residues are an aspartate and glutamate located on beta strands 4 and 7 respectively.
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
- Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 |
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Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. The Biochemist, vol. 30, no. 4., pp. 26-32. Download PDF version.