Biology:Guanylate kinase
| guanylate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 guanylate kinase homohexamer, E.Coli | |||||||||
| Identifiers | |||||||||
| EC number | 2.7.4.8 | ||||||||
| CAS number | 9026-59-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| guanylate kinase | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
 Structure of Guanylate Kinase.[1] | |||||||||||
| Identifiers | |||||||||||
| Symbol | Guanylate_kin | ||||||||||
| Pfam | PF00625 | ||||||||||
| InterPro | IPR008144 | ||||||||||
| PROSITE | PDOC00670 | ||||||||||
| SCOP2 | 1gky / SCOPe / SUPFAM | ||||||||||
| CDD | cd00071 | ||||||||||
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In enzymology, a guanylate kinase (EC 2.7.4.8) is an enzyme that catalyzes the chemical reaction
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
- ↑ 1.0 1.1 "Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0 A resolution". J. Mol. Biol. 224 (4): 1127–41. April 1992. doi:10.1016/0022-2836(92)90474-X. PMID 1314905.
- ↑ "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. February 1992. doi:10.1016/0092-8674(92)90136-Z. PMID 1310897.
- ↑ "Purification and sequence determination of guanylate kinase from pig brain". Eur. J. Biochem. 213 (1): 263–9. April 1993. doi:10.1111/j.1432-1033.1993.tb17757.x. PMID 8097461.
- ↑ 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.
- ↑ 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. PMID 33381848. PMC 7773487. https://doi.org/10.1093/bioinformatics/btaa813.
- ↑ 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. PMID 34073716.
- ↑ 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. PMID 36952396. PMC 10035753. https://journals.plos.org/ploscompbiol/article?id=10.1371/journal.pcbi.1010903.
Further reading
- "Partial purification and properties of ATP:GMP phosphotransferase from rat liver". Arch. Biochem. Biophys. 132 (1): 49–61. 1969. doi:10.1016/0003-9861(69)90337-3. PMID 4307347.
- "Nucleoside monophosphokinases of Escherichia coli infected and uninfected with an RNA phage". Biochim. Biophys. Acta 114 (2): 416–8. 1966. doi:10.1016/0005-2787(66)90324-8. PMID 5329274.
- "The partial purification of deoxynucleoside monophosphate kinases from L cells". Biochim. Biophys. Acta 108 (1): 114–24. 1965. doi:10.1016/0005-2787(65)90113-9. PMID 5862227.
- "Purification and properties of guanylate kinase from Escherichia coli". J. Biol. Chem. 241 (22): 5452–60. 1966. doi:10.1016/S0021-9258(18)96451-3. PMID 5333666.
- "Metabolism of deoxyribonucleotides. Purification and properties of deoxyguanosine monophosphokinase of calf thymus". Eur. J. Biochem. 19 (2): 256–63. 1971. doi:10.1111/j.1432-1033.1971.tb01312.x. PMID 5552394.
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