PMID:8869631

Citation	Banerjee, S, Anderson, F and Farber, GK (1995) The evolution of sugar isomerases. Protein Eng. 8:1189-95
Abstract	L-Arabinose isomerase (EC 5.3.1.4) catalyzes the isomerization of L-arabinose to L-ribulose. Here we report on the purification, kinetic mechanism and chemical mechanism of L-arabinose isomerase from Escherichia coli. The enzyme catalyzes the isomerization of L-arabinose to L-ribulose by a proton transfer mechanism, in contrast to xylose isomerase which uses a hydride transfer mechanism to perform a similar isomerization. Arabinose isomerase activity is metal dependent, although the enzyme can catalyze the exchange of the proton attached to carbon 2 of arabinose with the solvent in the absence of metal ion. Manganese(II) is the only metal ion which renders the enzyme active for the isomerization reaction. Arabinose isomerase has high substrate specificity for L-arabinose. The difference in chemical mechanism between xylose isomerase and arabinose isomerase suggests that these enzymes are not related by convergent evolution. This work also suggests that unless convergent evolution has been demonstrated, the mechanism of one enzyme may not give any insight into the mechanism of a second enzyme catalyzing the same reaction.
Links	PubMed
Keywords	Aldose-Ketose Isomerases; Binding Sites; Carbohydrate Epimerases/isolation & purification; Carbohydrate Epimerases/metabolism; Escherichia coli/enzymology; Evolution, Molecular; Kinetics; Magnetic Resonance Spectroscopy; Models, Chemical; Molecular Structure; Pentoses/chemistry; Pentoses/metabolism; Protons
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