An Unusual His/Asp Dyad Operates Catalysis in Agar-Degrading Glycosidases
Mert Sagiroglugil, Alba Nin-Hill, Elizabeth Ficko-Blean, Carme Rovira · 2024
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Description
A peer-reviewed research article from Europe PMC (2024). Agarose motifs, found in agars present in the cell walls of red algae, consist of alternating units of d-galactose (G) and α-3,6-anhydro-l-galactose (LA). Glycoside hydrolases from family 117 (GH117) cleave the terminal α-1,3-glycosidic bonds, releasing LA units. Structural studies have suggested that these enzymes use unconventional catalytic machinery, involving a histidine (His302) as a general acid rather than a carboxylic residue as in most glycosidases.
Catalog record
| CREATOR | Mert Sagiroglugil, Alba Nin-Hill, Elizabeth Ficko-Blean, Carme Rovira |
|---|---|
| YEAR | 2024 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 30 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |