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GTP diphosphokinase

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GTP diphosphokinase
Identifiers
EC no.2.7.6.5
CAS no.63690-89-1
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

GTP diphosphokinase (EC 2.7.6.5) is an enzyme that catalyzes the chemical reaction

The enzyme characterised from species of Bacillus converts guanosine triphosphate (GTP) to guanosine 3'-diphosphate 5'-triphosphate by transferring a pyrophosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine monophosphate (AMP).[1][2]

Nomenclature

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This enzyme is a transferase, specifically one transferring two phosphorus-containing groups (diphosphotransferases). The systematic name of this enzyme class is ATP:GTP 3'-diphosphotransferase. Other names in common use include stringent factor, guanosine 3',5'-polyphosphate synthase, GTP pyrophosphokinase, ATP-GTP 3'-diphosphotransferase, guanosine 5',3'-polyphosphate synthetase, (p)ppGpp synthetase I, (p)ppGpp synthetase II, guanosine pentaphosphate synthetase, GPSI, and GPSII.[3]

Structural studies

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As of late 2007, 4 structures have been solved for this class of enzymes, with Protein Data Bank accession codes PDB: 1E3H​, PDB: 1E3P​, PDB: 1VJ7​, and PDB: 2BE3​.

References

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  1. ↑ Sy J, Akers H (1976). "Purification and properties of guanosine 5', 3'-polyphosphate synthetase from Bacillus brevis". Biochemistry. 15 (20): 4399–403. doi:10.1021/bi00665a008. PMID 184817.
  2. ↑ Fehr S, Richter D (1981). "Stringent response of Bacillus stearothermophilus: evidence for the existence of two distinct guanosine 3',5'-polyphosphate synthetases". J. Bacteriol. 145 (1): 68–73. doi:10.1128/JB.145.1.68-73.1981. PMC 217245. PMID 6161916.
  3. ↑ Enzyme 2.7.6.5 at KEGG Pathway Database.