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Keywords:

  • enzyme catalysis;
  • enzyme enantioselectivity;
  • enzyme inhibitors;
  • guanosine monophosphate synthetase;
  • kinetics
Thumbnail image of graphical abstract

Mirror, mirror…? The enantioselectivity of guanosine monophosphate synthetase (GMPS), a key enzyme in GMP biosynthesis, was characterized by using D- and L-xanthosine 5′-monophosphate (XMP) as substrates. L-XMP was found to be converted to L-GMP by E. coli GMPS and to inhibit enzymatic activity. These results provide insight into GMPS–ligand interactions that might be useful in future inhibitor design.