| Activities in Family | L-Rhα-α-1,4-GlcA-specific α-L-rhamnosidase (EC 3.2.1.-) |
|---|---|
| Mechanism | Retaining |
| 3D Structure Status | seven-bladed β-propeller |
| Catalytic Nucleophile/Base | His |
| Note | Created after Munoz-Munoz et al., Proc. Natl. Acad. Sci. USA (2017) (PMID=28396425); these enzymes hydrolyze a-L-rhamnose residues linked to position 4 of a glucuronic acid using an unusual catalytic machinery comprising a histidine residue. The active site of these a-L-rhamnosidases is located on the opposite side of CAZymes with similar b-propeller folds. Surprisingly, the "normal" side of the b-propeller bears the highest residue conservation in the family and may well have another function. The latter is unknown but strong ressemblance to family PL25 suggests a polysaccharide lyase activity. |
| Statistics | GenBank accession (91); Uniprot accession (1); PDB accession (5); 3D entries (4); cryst (0) |