Sugar transporters from bacteria, parasites and mammals: structure-activity relationships

Trends Biochem Sci. 1998 Dec;23(12):476-81. doi: 10.1016/s0968-0004(98)01326-7.


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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Biological Transport
  • Calcium-Binding Proteins*
  • Carbohydrate Metabolism*
  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism*
  • Cytochalasin B / metabolism
  • Glucose Transporter Type 1
  • Mammals
  • Molecular Sequence Data
  • Monosaccharide Transport Proteins / chemistry
  • Monosaccharide Transport Proteins / metabolism
  • Parasites
  • Periplasmic Binding Proteins*
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Structure-Activity Relationship


  • Bacterial Proteins
  • Calcium-Binding Proteins
  • Carrier Proteins
  • Glucose Transporter Type 1
  • Monosaccharide Transport Proteins
  • Periplasmic Binding Proteins
  • galactose-binding protein
  • Cytochalasin B