Guanylate_kinase

Guanylate kinase

Guanylate kinase

Enzyme

In enzymology, a guanylate kinase (EC 2.7.4.8) is an enzyme that catalyzes the chemical reaction

ATP + GMP ADP + GDP
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Thus, the two substrates of this enzyme are ATP and GMP, whereas its two products are ADP and GDP.

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

  1. [1]
    Stehle 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. PMID 1314905.
  2. [2]
    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. PMID 1310897. S2CID 46607652.
  3. [3]
    Zschocke PD, Schiltz E, Schulz GE (April 1993). "Purification and sequence determination of guanylate kinase from pig brain". Eur. J. Biochem. 213 (1): 263–9. doi:10.1111/j.1432-1033.1993.tb17757.x. PMID 8097461.
  4. [4]
    Goebl MG (March 1992). "Is the erythrocyte protein p55 a membrane-bound guanylate kinase?". Trends Biochem. Sci. 17 (3): 99. doi:10.1016/0968-0004(92)90244-4. PMID 1329277.
  5. [5]
    Renz, Alina; Widerspick, Lina; Dräger, Andreas (2020). "FBA reveals guanylate kinase as a potential target for antiviral therapies against SARS-CoV-2". Bioinformatics. 36 (Supplement_2): i813–i821. doi:10.1093/bioinformatics/btaa813. PMC 7773487. PMID 33381848. S2CID 229929774.
  6. [6]
    Renz, Alina; Widerspick, Lina; Dräger, Andreas (2021). "Genome-Scale Metabolic Model of Infection with SARS-CoV-2 Mutants Confirms Guanylate Kinase as Robust Potential Antiviral Target". Genes. 12 (6): 796. doi:10.3390/genes12060796. PMC 8225150. PMID 34073716. S2CID 235300463.
  7. [7]
    Leonidou, Nantia; Renz, Alina; Mostolizadeh, Reihaneh; Dräger, Andreas (2023). "New workflow predicts drug targets against SARS-CoV-2 via metabolic changes in infected cells". PLOS Computational Biology. 19 (3): 1–32. doi:10.1371/journal.pcbi.1010903. PMC 10035753. PMID 36952396. S2CID 257715107.

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR008144


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