EC Number   |
Reference |
|---|
   5.4.99.62 | to 1.9 A resolution. Protein assembles into four different oligomeric forms, among which the smallest homodimeric form is most abundant and would be the predominant species under physiological conditions. This homodimer has two fucose-binding sites that are devoid of the His-Asp dyad and catalytically inactive, indicating that the mutarotase and the pyranase activities appear dispensable in vertebrates |
725706 |
| 5.4.99.62 | to 1.9 A resolution. Protein forms a decameric toroid with each active site formed by two adjacent subunits. While one subunit provides most of the fucose-interacting residues including a catalytic tyrosine residue, the other subunit provides a catalytic His-Asp dyad. This active-site feature is critical both for the mutarotase activity toward L-fucose and for the pyranase activity toward D-ribose |
725706 |
| 5.4.99.62 | to 2.3 A resolution. Protein shows a decameric toroidal assembly. The intersubunit cleft of the protein binds specific forms of D-ribose, but it does not have an enzyme activity toward the sugar |
729962 |
