Guanylate kinase

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guanylate kinase
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 / EGO
guanylate kinase
PDB 1gky EBI.jpg
Structure of Guanylate Kinase.[1]
Identifiers
Symbol Guanylate_kin
Pfam PF00625
InterPro IPR008144
PROSITE PDOC00670
SCOP 1gky
SUPERFAMILY 1gky

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

ATP + GMP \rightleftharpoons 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]

Nomenclature[edit]

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[edit]

  1. ^ a b 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. 
  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. 

Further reading[edit]

  • Buccino RJ Jr, Roth JS (1969). "Partial purification and properties of ATP:GMP phosphransferase from rat liver". Arch. Biochem. Biophys. 132 (1): 49–61. doi:10.1016/0003-9861(69)90337-3. PMID 4307347. 
  • Hiraga S, Sugino Y (1966). "Nucleoside monophosphokinases of Escherichia coli infected and uninfected with an RNA phage". Biochim. Biophys. Acta. 114 (2): 416–8. doi:10.1016/0005-2787(66)90324-8. PMID 5329274. 
  • Griffith TJ, Helleiner CW (1965). "The partial purification of deoxynucleoside monophosphate kinases from L cells". Biochim. Biophys. Acta. 108 (1): 114–24. PMID 5862227. 
  • Oeschger MP, Bessman MJ (1966). "Purification and properties of guanylate kinase from Escherichia coli". J. Biol. Chem. 241 (22): 5452–60. PMID 5333666. 
  • Shimono H, Sugino Y (1971). "Metabolism of deoxyribonucleotides. Purification and properties of deoxyguanosine monophosphokinase of calf thymus". Eur. J. Biochem. 19 (2): 256–63. doi:10.1111/j.1432-1033.1971.tb01312.x. PMID 5552394. 

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