| L-fucose isomerase | |
| Ec Number: | 5.3.1.25 |
| Cas Number: | 60063-83-4 |
| Go Code: | 0008736 |
| Symbol: | Fucose_iso_N1 |
| L-fucose isomerase, first N-terminal domain | |
| Pfam: | PF07881 |
| Interpro: | IPR012888 |
| Scop: | 1fui |
| Symbol: | Fucose_iso_N2 |
| L-fucose isomerase, second N-terminal domain | |
| Pfam: | PF07882 |
| Interpro: | IPR012889 |
| Scop: | 1fui |
| Symbol: | Fucose_iso_C |
| L-fucose isomerase, C-terminal domain | |
| Pfam: | PF02952 |
| Pfam Clan: | CL0393 |
| Interpro: | IPR015888 |
| Scop: | 1fui |
In enzymology, a L-fucose isomerase is an enzyme that catalyzes the chemical reaction
L-fucose
\rightleftharpoons
Hence, this enzyme has one substrate, L-fucose, and one product, L-fuculose.
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is L-fucose aldose-ketose-isomerase. This enzyme participates in fructose and mannose metabolism.
The enzyme is a hexamer, forming the largest structurally known ketol isomerase, and has no sequence or structural similarity with other ketol isomerases. The structure was determined by X-ray crystallography at 2.5 Angstrom resolution.[1] Each subunit of the hexameric enzyme is wedge-shaped and composed of three domains. Both domains 1 and 2 contain central parallel beta- sheets with surrounding alpha helices. The active centre is shared between pairs of subunits related along the molecular three-fold axis, with domains 2 and 3 from one subunit providing most of the substrate-contacting residues.