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Abstract
Sugar transport across the plasma membrane is one of the most important transport
processes. The cloning and expression of cDNAs from a superfamily of related sugar
transporters that all adopt a 12-membrane-spanning-domain structure has opened new
avenues of investigation, including presteady-state kinetic analysis. Structure-function
analyses of mammalian and bacterial sugar transporters, and comparisons of these transporters
with those of parasitic trypanosomatids, indicate that different environmental pressures
have tailored the evolution of the various members of the sugar-transporter superfamily.
Subtle distinctions in the function of these proteins can be related to particular
amino acid residue substitutions.