| Type: | Family | Name: | Xylose isomerase |
| Description: | Xylose isomerase () [] is an enzyme found in microorganisms which catalyzes the interconversion of D-xylose to D-xylulose. It can also isomerize D-ribose to D-ribulose and D-glucose to D-fructose. The enzyme is a homotetramer, which is stabilised by cobalt, and requires magnesium for its catalytic activity. Each subunit contains 2 domains: the core domain is a parallel alpha-beta barrel; the C-terminal domain is a loop structure consisting of 5 helices and is involved in intermolecular contacts between adjacent subunits []. The active site lies in a deep pocket near the C-terminal ends of the strands of the barrel domain and includes residues from a second subunit. The tetramer is effectively a dimer of "active" dimers, the active sites being composed of residues from both subunits [].Xylose isomerase also exists in plants [] where it is homodimeric and is manganese-dependent. | Short Name: | Xylose_isomerase |
