In enzymology, a L-fucose isomerase (EC 5.3.1.25) is an enzyme that catalyzes the chemical reaction

L-fucose L-fuculose

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.[1]

References

  1. ^ a b Seemann JE, Schulz GE (October 1997). "Structure and mechanism of L-fucose isomerase from Escherichia coli". J. Mol. Biol. 273 (1): 256–68. doi:10.1006/jmbi.1997.1280. PMID 9367760.

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR015888
This article incorporates text from the public domain Pfam and InterPro: IPR012889
This article incorporates text from the public domain Pfam and InterPro: IPR012888


Allikas: http://en.wikipedia.org/wiki/L-fucose_isomerase
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