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 . The enzyme catalyses the aldose-ketose isomerization of several sugars. Most enzymes also catalyse the reaction of EC 18.104.22.168, L-fucose isomerase . The enzyme from the bacterium Falsibacillus pallidus also converts D-altrose to D-psicose . cf. EC 22.214.171.124, L-arabinose isomerase.
Cohen, S.S. Studies on D-ribulose and its enzymatic conversion to D-arabinose. J. Biol. Chem.201 (1953) 71–84. [PMID: 13044776]
Green, M. and Cohen, S.S. Enzymatic conversion of L-fucose to L-fuculose. J. Biol. Chem.219 (1956) 557–568. [PMID: 13319278]
Seemann, J.E. and Schulz, G.E. Structure and mechanism of L-fucose isomerase from Escherichia coli. J. Mol. Biol.273 (1997) 256–268. [DOI] [PMID: 9367760]
Takeda, K., Yoshida, H., Izumori, K. and Kamitori, S. X-ray structures of Bacillus pallidus D-arabinose isomerase and its complex with L-fucitol. Biochim. Biophys. Acta1804 (2010) 1359–1368. [DOI] [PMID: 20123133]