1H, 13C and 15N resonance assignment of human guanylate kinase
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.
KeywordsEnzyme Guanylate kinase (GMPK) NMR assignment Nucleotide kinase
We thank Prof. Dr. Christian Griesinger for providing measurement time and for valuable discussions related to the project. This research was supported by a DAAD scholarship (to NK), the Max Planck Society and by start-up funds provided by the James Graham Brown Foundation.
- Keller RL (2004) Computer aided resonance assignment. http://cara.nmr.ch/ Accessed 26 July 2016
- Konrad M (1992) Cloning and expression of the essential gene for guanylate kinase from yeast. J Biol Chem 267:25652–25655Google Scholar
- Marion D, Driscoll PC, Kay LE et al (1989a) Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1β. BioChemistry 28:6150–6156CrossRefGoogle Scholar
- Miller WH, Miller RL (1980) Phosphorylation of acyclovir (acycloguanosine) monophosphate by GMP kinase. J Biol Chem 255:7204–7207Google Scholar