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Inhibition of Guanosine Monophosphate Synthetase by the Substrate Enantiomer L ‐XMP
Author(s) -
Struntz Nicholas B.,
Hu Tianshun,
White Brian R.,
Olson Margaret E.,
Harki Daniel A.
Publication year - 2012
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201200503
Subject(s) - chemistry , nucleotide , guanosine , enzyme , stereochemistry , biochemistry , nucleoside , guanosine monophosphate , ligand (biochemistry) , biosynthesis , receptor , gene
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.