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Glycoside Hydrolase Family 125
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- 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
Kinetic characterization of 2,4-dinitrophenyl a-D-mannopyranoside hydrolysis by SpGH125 and Cp125 revealed that this is a poor substrate for these enzymes. Monitoring the hydrolysis of methyl 6-O-(α-D-mannopyranosyl)-β-D-mannopyranoside sup>1H NMR spectroscopy revealed that CpGH125 and SpGH125 act with inversion of stereochemistry
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 |