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Difference between revisions of "Glycoside Hydrolase Family 125"
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== Substrate specificities == | == Substrate specificities == | ||
| − | + | The currently characterized family 125 glycoside hydrolyses, which include the examples from ''Streptococcus pneumoniae'' (SpGH125) and ''Clostridium perfringens'' (CpGH125), are a-mannosidases with specificity for a-1,6-linked non-reducing terminal mannose residues. | |
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Revision as of 08:56, 16 November 2012
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: ^^^Alisdair Boraston^^^
- Responsible Curator: ^^^Alisdair Boraston^^^
| Glycoside Hydrolase Family GH125 | |
| Clan | GH-L |
| Mechanism | inverting |
| Active site residues | known |
| CAZy DB link | |
| https://www.cazy.org/GH125.html | |
Substrate specificities
The currently characterized family 125 glycoside hydrolyses, which include the examples from Streptococcus pneumoniae (SpGH125) and Clostridium perfringens (CpGH125), are a-mannosidases with specificity for a-1,6-linked non-reducing terminal mannose residues.
Kinetics and Mechanism
Content is to be added here.
Catalytic Residues
Content is to be added here.
Three-dimensional structures
Content is to be added here.
Family Firsts
- First stereochemistry determination
- 1H NMR spectroscopy revealed that CpGH125 and SpGH125 act with inversion of stereochemistry [1]..
- First catalytic nucleophile identification
- Cite some reference here, with a short (1-2 sentence) explanation [2].
- First general acid/base residue identification
- Cite some reference here, with a short (1-2 sentence) explanation [3].
- First 3-D structure
- Cite some reference here, with a short (1-2 sentence) explanation [4].
References
- Gregg KJ, Zandberg WF, Hehemann JH, Whitworth GE, Deng L, Vocadlo DJ, and Boraston AB. (2011). Analysis of a new family of widely distributed metal-independent alpha-mannosidases provides unique insight into the processing of N-linked glycans. J Biol Chem. 2011;286(17):15586-96. DOI:10.1074/jbc.M111.223172 |