| Affiliation: | 1.James Graham Brown Cancer Center, Department of Medicine,University of Louisville,Louisville,USA;2.Enzyme Biochemistry Group,Max Planck Institute for Biophysical Chemistry,G?ttingen,Germany;3.Department for NMR-Based Structural Biology,Max Planck Institute for Biophysical Chemistry,G?ttingen,Germany;4.ZoBio B.V.,Leiden,The Netherlands |
| Abstract: | Human guanylate kinase (hGMPK) is a critical enzyme that, in addition to phosphorylating its physiological substrate (d)GMP, catalyzes the second phosphorylation step in the conversion of anti-viral and anti-cancer nucleoside analogs to their corresponding active nucleoside analog triphosphates. Until now, a high-resolution structure of hGMPK is unavailable and thus, we studied free hGMPK by NMR and assigned the chemical shift resonances of backbone and side chain 1H, 13C, and 15N nuclei as a first step towards the enzyme’s structural and mechanistic analysis with atomic resolution. |
