EC 5.3.1.25 - L-fucose isomerase

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IntEnz Enzyme Nomenclature
EC 5.3.1.25

Names

Accepted name:
L-fucose isomerase
Other name:
L-fucose ketol-isomerase
Systematic name:
L-fucose aldose-ketose-isomerase

Reaction

Cofactor

Comments:

Requires a divalent metal ion (the enzyme from the bacterium Escherichia coli prefers Mn2+). The enzyme binds the closed form of the sugar and catalyses ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism [3]. The enzyme from Escherichia coli can also convert D-arabinose to D-ribulose [1]. The enzyme from the thermophilic bacterium Caldicellulosiruptor saccharolyticus also converts D-altrose to D-psicose and L-galactose to L-tagatose [4].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ERGO , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008736
UniProtKB/Swiss-Prot: (60) [show] [UniProt]

References

  1. GREEN, M., COHEN, S. S.
    Enzymatic conversion of L-fucose to L-fuculose.
    J. Biol. Chem. 219: 557-568 (1956). [PMID: 13319278]
  2. Lu, Z. and Lin, E.C.C.
    The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation.
    Nucleic Acids Res. 17: 4883-4884 (1989). [PMID: 2664711]
  3. Seemann, J. E., Schulz, G. E.
    Structure and mechanism of L-fucose isomerase from Escherichia coli.
    J. Mol. Biol. 273: 256-268 (1997). [PMID: 9367760]
  4. Ju, Y. H., Oh, D. K.
    Characterization of a recombinant L-fucose isomerase from Caldicellulosiruptor saccharolyticus that isomerizes L-fucose, D-arabinose, D-altrose, and L-galactose.
    Biotechnol. Lett. 32: 299-304 (2010). [PMID: 19856146]

[EC 5.3.1.25 created 1999]