This enzyme belongs to the family of
transferases, specifically those transferring phosphorus-containing groups (
phosphotransferases) with a phosphate group as acceptor. This enzyme participates in
purine metabolism.
Guanylate kinase catalyzes the ATP-dependent phosphorylation of GMP into GDP.[1] It is essential for recycling GMP and indirectly,
cGMP. In prokaryotes (such as Escherichia coli), lower eukaryotes (such as yeast) and in vertebrates, GK is a highly conserved monomeric protein of about 200 amino acids. GK has been shown to be structurally similar to protein A57R (or SalG2R) from various strains of
Vaccinia virus.[2][3][4]Systems biology analyses carried out by the team of
Andreas Dräger also identified a pivotal role of this enzyme in the replication of
SARS-CoV-2 within the human airways.[5][6][7]
Nomenclature
The
systematic name of this enzyme class is ATP:(d)GMP phosphotransferase. Other names in common use include"
deoxyguanylate kinase,
5'-GMP kinase,
GMP kinase,
guanosine monophosphate kinase, and
ATP:GMP phosphotransferase.
References
^
abStehle T, Schulz GE (April 1992). "Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0 A resolution". J. Mol. Biol. 224 (4): 1127–41.
doi:
10.1016/0022-2836(92)90474-X.
PMID1314905.
^Bryant PJ, Woods DF (February 1992). "A major palmitoylated membrane protein of human erythrocytes shows homology to yeast guanylate kinase and to the product of a Drosophila tumor suppressor gene". Cell. 68 (4): 621–2.
doi:
10.1016/0092-8674(92)90136-Z.
PMID1310897.
S2CID46607652.