Guanylate kinase

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guanylate kinase
2an9.jpg
guanylate kinase homohexamer, E.Coli
Identifiers
EC no. 2.7.4.8
CAS no. 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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PMC articles
PubMed articles
NCBI proteins
guanylate kinase
PDB 1gky EBI.jpg
Structure of Guanylate Kinase. [1]
Identifiers
SymbolGuanylate_kin
Pfam PF00625
InterPro IPR008144
PROSITE PDOC00670
SCOP2 1gky / SCOPe / SUPFAM
CDD cd00071
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
PDB 1ex6 , 1ex7 , 1gky , 1jxm , 1jxo , 1kgd , 1kjw , 1lvg , 1s4q , 1s96 , 1xzp , 1xzq , 1z6g , 1z8f , 1znw , 1znx , 1zny , 1znz , 2an9 , 2anb , 2anc , 2f3r , 2f3t , 2qor

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

Contents

ATP + GMP ADP + GDP

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"

Related Research Articles

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References

  1. 1 2 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. 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. 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. 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. 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. 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. 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