The Enzyme Database

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EC 5.3.1.25     
Accepted name: L-fucose isomerase
Reaction: L-fucopyranose = L-fuculose
Systematic name: L-fucose aldose-ketose-isomerase
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: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60063-83-4
References:
1.  Green, M. and Cohen, S.S. Enzymatic conversion of L-fucose to L-fuculose. J. Biol. Chem. 219 (1956) 557–568. [PMID: 13319278]
2.  Lu, Z., Lin, E.C.C. The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation. Nucleic Acids Res. 17 (1989) 4883–4884. [PMID: 2664711]
3.  Seemann, J.E. and Schulz, G.E. Structure and mechanism of L-fucose isomerase from Escherichia coli. J. Mol. Biol. 273 (1997) 256–268. [PMID: 9367760]
4.  Ju, Y.H. and 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 (2010) 299–304. [PMID: 19856146]
[EC 5.3.1.25 created 1999]
 
 


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