Record Information
Version2.0
Creation Date2012-05-31 13:48:52 -0600
Update Date2015-09-13 12:56:10 -0600
Secondary Accession Numbers
  • ECMDB01273
Identification
Name:Guanosine triphosphate
Description:Guanosine triphosphate (GTP) is a guanine nucleotide containing three phosphate groups esterified to the sugar moiety. GTP functions as a carrier of phosphates and pyrophosphates involved in channeling chemical energy into specific biosynthetic pathways. GTP activates the signal transducing G proteins which are involved in various cellular processes including proliferation, differentiation, and activation of several intracellular kinase cascades. Proliferation and apoptosis are regulated in part by the hydrolysis of GTP by small GTPases Ras and Rho. Another type of small GTPase, Rab, plays a role in the docking and fusion of vesicles and may also be involved in vesicle formation. In addition to its role in signal transduction, GTP also serves as an energy-rich precursor of mononucleotide units in the enzymatic biosynthesis of DNA and RNA.
Structure
Thumb
Synonyms:
  • 5'-GTP
  • GTG
  • GTP
  • Guanosine 5'-(tetrahydrogen triphosphate)
  • Guanosine 5'-(tetrahydrogen triphosphoric acid)
  • Guanosine 5'-triphosphate
  • Guanosine 5'-triphosphorate
  • Guanosine 5'-triphosphoric acid
  • Guanosine mono(tetrahydrogen triphosphate) (ester)
  • Guanosine mono(tetrahydrogen triphosphoric acid) (ester)
  • Guanosine Triphosphate
  • Guanosine triphosphoric acid
  • Guanosine-triphosphate
  • Guanosine-triphosphoric acid
  • Guanylyl imidodiphosphate
  • Guanylyl imidodiphosphoric acid
  • H4gtp
Chemical Formula:C10H16N5O14P3
Weight:Average: 523.1804
Monoisotopic: 522.990659781
InChI Key:XKMLYUALXHKNFT-UUOKFMHZSA-N
InChI:InChI=1S/C10H16N5O14P3/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(27-9)1-26-31(22,23)29-32(24,25)28-30(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H,24,25)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1
CAS number:86-01-1
IUPAC Name:({[({[(2R,3S,4R,5R)-5-(2-amino-6-oxo-6,9-dihydro-1H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)phosphonic acid
Traditional IUPAC Name:triphosphate, guanosine
SMILES:NC1=NC2=C(N=CN2[C@@H]2O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]2O)C(=O)N1
Chemical Taxonomy
DescriptionThis compound belongs to the class of chemical entities known as purine ribonucleoside triphosphates. These are purine ribobucleotides with a triphosphate group linked to the ribose moiety.
KingdomChemical entities
Super ClassOrganic compounds
ClassNucleosides, nucleotides, and analogues
Sub ClassPurine nucleotides
Direct ParentPurine ribonucleoside triphosphates
Alternative Parents
Substituents
  • Purine ribonucleoside triphosphate
  • Purine ribonucleoside monophosphate
  • Pentose phosphate
  • Pentose-5-phosphate
  • Glycosyl compound
  • N-glycosyl compound
  • Monosaccharide phosphate
  • Imidazopyrimidine
  • Purine
  • Hydroxypyrimidine
  • Monoalkyl phosphate
  • Monosaccharide
  • N-substituted imidazole
  • Organic phosphoric acid derivative
  • Phosphoric acid ester
  • Pyrimidine
  • Alkyl phosphate
  • Azole
  • Heteroaromatic compound
  • Oxolane
  • Imidazole
  • Secondary alcohol
  • 1,2-diol
  • Organoheterocyclic compound
  • Azacycle
  • Oxacycle
  • Organic oxide
  • Organopnictogen compound
  • Organooxygen compound
  • Organic nitrogen compound
  • Hydrocarbon derivative
  • Organic oxygen compound
  • Organonitrogen compound
  • Alcohol
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors
Physical Properties
State:Solid
Charge:-3
Melting point:Not Available
Experimental Properties:
PropertyValueSource
Predicted Properties
PropertyValueSource
Water Solubility10.4 mg/mLALOGPS
logP-0.63ALOGPS
logP-3.6ChemAxon
logS-1.7ALOGPS
pKa (Strongest Acidic)0.8ChemAxon
pKa (Strongest Basic)1.57ChemAxon
Physiological Charge-3ChemAxon
Hydrogen Acceptor Count14ChemAxon
Hydrogen Donor Count8ChemAxon
Polar Surface Area294.81 Å2ChemAxon
Rotatable Bond Count8ChemAxon
Refractivity97.24 m3·mol-1ChemAxon
Polarizability39.81 Å3ChemAxon
Number of Rings3ChemAxon
Bioavailability0ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
2 Flavodoxin reduced + Guanosine triphosphate + 2 Hydrogen ion > dGTP +2 flavodoxin semi oxidized + Water
Guanosine triphosphate + Water > Guanosine monophosphate + Hydrogen ion + Pyrophosphate
Adenosine triphosphate + Guanosine diphosphate <> ADP + Guanosine triphosphate
Guanosine triphosphate + Water <> Cyclic pyranopterin monophosphate + Pyrophosphate
Adenosine triphosphate + Guanosine triphosphate + Water + Sulfate > Adenosine phosphosulfate + Guanosine diphosphate + Phosphate + Pyrophosphate
bis-molybdenum cofactor + Guanosine triphosphate + Hydrogen ion > bis-molybdopterin mono-guanine dinucleotide + Pyrophosphate
Guanosine triphosphate + Hydrogen ion + Molybdopterin > Molybdopterin guanine dinucleotide + Pyrophosphate
bis-molybdopterin mono-guanine dinucleotide + Guanosine triphosphate + Hydrogen ion > Bis-molybdopterin guanine dinucleotide + Pyrophosphate
tungsten bispterin cofactor + Guanosine triphosphate + Hydrogen ion > tungsten bispterin cofactor mono-guanine dinucleotide + Pyrophosphate
tungsten bispterin cofactor mono-guanine dinucleotide + Guanosine triphosphate + Hydrogen ion > tungsten bispterin cofactor guanine dinucleotide + Pyrophosphate
Guanosine triphosphate + Water > Guanosine + Triphosphate
Adenosine monophosphate + Guanosine triphosphate <> ADP + Guanosine diphosphate
Guanosine triphosphate + Water > Guanosine diphosphate + Hydrogen ion + Phosphate
Guanosine triphosphate + 3 Water <> 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Formic acid +2 Hydrogen ion + Pyrophosphate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine
Adenosyl cobinamide phosphate + Guanosine triphosphate + Hydrogen ion > Adenosylcobinamide-GDP + Pyrophosphate
Cytidine + Guanosine triphosphate > Cytidine monophosphate + Guanosine diphosphate + Hydrogen ion
Guanosine triphosphate + Uridine > Guanosine diphosphate + Hydrogen ion + Uridine 5'-monophosphate
Guanosine triphosphate + Water > Dihydroneopterin triphosphate + Formic acid + Hydrogen ion
Adenosine triphosphate + Guanosine triphosphate <> Adenosine monophosphate + Guanosine 3'-diphosphate 5'-triphosphate + Hydrogen ion
Guanosine 3'-diphosphate 5'-triphosphate + Water > Guanosine triphosphate + Pyrophosphate
Guanosine triphosphate + Water > Guanosine diphosphate + Hydrogen ion + Phosphate
L-Aspartic acid + Guanosine triphosphate + Inosinic acid <> Adenylsuccinic acid + Guanosine diphosphate +2 Hydrogen ion + Phosphate
Guanosine triphosphate + Hydrogen ion + Water > Ammonium + Xanthosine 5-triphosphate
Adenosine triphosphate + Guanosine diphosphate <> ADP + Guanosine triphosphate
Guanosine triphosphate + 3 Water <> Formic acid + 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Pyrophosphate
Guanosine triphosphate + Water <> Guanosine monophosphate + Pyrophosphate
Guanosine triphosphate + Water <> Formamidopyrimidine nucleoside triphosphate
Adenosine triphosphate + Guanosine triphosphate <> Adenosine monophosphate + Guanosine 3'-diphosphate 5'-triphosphate
Guanosine triphosphate + Pyruvic acid <> Guanosine diphosphate + Phosphoenolpyruvic acid
Guanosine triphosphate <> Cyclic GMP + Pyrophosphate
Guanosine triphosphate + RNA <> Pyrophosphate + RNA
Guanosine triphosphate + Cytidine <> Guanosine diphosphate + Cytidine monophosphate
Guanosine triphosphate + D-Mannose 1-phosphate <> Pyrophosphate + Guanosine diphosphate mannose
Guanosine triphosphate + Uridine <> Guanosine diphosphate + Uridine 5'-monophosphate
Guanosine triphosphate + Inosinic acid + L-Aspartic acid <> Guanosine diphosphate + Phosphate + Adenylsuccinic acid
dGTP + Thioredoxin disulfide + Water <> Guanosine triphosphate + Thioredoxin
Adenosyl cobinamide phosphate + Guanosine triphosphate <> Adenosylcobinamide-GDP + Pyrophosphate
Adenosyl cobinamide + Guanosine triphosphate <> Adenosyl cobinamide phosphate + Guanosine diphosphate
2 Guanosine triphosphate <> 3',5'-Cyclic diGMP +2 Pyrophosphate + Cyclic di-3',5'-guanylate
Guanosine triphosphate + Water <> Cyclic pyranopterin monophosphate + Pyrophosphate
Guanosine triphosphate + hydroxyl radical > Hydrogen ion + 8-oxo-GTP
Hydrogen ion + D-Mannose 1-phosphate + Guanosine triphosphate > Guanosine diphosphate mannose + Pyrophosphate
Guanosine triphosphate + Water > Hydrogen ion + Guanosine diphosphate + Phosphate
L-Aspartic acid + Inosinic acid + Guanosine triphosphate > Hydrogen ion + adenylo-succinate + Phosphate + Guanosine diphosphate
Hydrogen ion + Adenosyl cobinamide phosphate + Guanosine triphosphate > Adenosylcobinamide-GDP + Pyrophosphate
Cytidine + Guanosine triphosphate > Hydrogen ion + Cytidine monophosphate + Guanosine diphosphate
Guanosine diphosphate + Adenosine triphosphate > Guanosine triphosphate + ADP
Guanosine triphosphate + Water > Hydrogen ion + Formic acid + Dihydroneopterin triphosphate
Water + Guanosine triphosphate > Hydrogen ion + Pyrophosphate + 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Formic acid
Guanosine triphosphate + Adenosine triphosphate > Guanosine 3'-diphosphate 5'-triphosphate + Adenosine monophosphate
Guanosine triphosphate <> Cyclic GMP + Pyrophosphate
Guanosine triphosphate > Cyclic pyranopterin monophosphate + Pyrophosphate
Hydrogen ion + molybdenum cofactor + Guanosine triphosphate <> Molybdopterin guanine dinucleotide + Pyrophosphate
Guanosine triphosphate > cyclic di-3',5'-guanylate + Pyrophosphate
Guanosine triphosphate + Water > Hydrogen ion + Guanosine diphosphate + Phosphate
Guanosine 3'-diphosphate 5'-triphosphate + Water > Hydrogen ion + Guanosine triphosphate + Pyrophosphate
Uridine + Guanosine triphosphate > Hydrogen ion + Uridine 5'-monophosphate + Guanosine diphosphate
2 Guanosine triphosphate >2 Pyrophosphate + Cyclic di-3',5'-guanylate
Guanosine triphosphate + adenosylcobinamide phosphate > Pyrophosphate + Adenosylcobinamide-GDP
2 Guanosine triphosphate >2 Pyrophosphate + Cyclic di-3',5'-guanylate
Guanosine triphosphate + Water > Formic acid + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
Guanosine triphosphate + Water > Guanosine diphosphate + Inorganic phosphate
Guanosine triphosphate + Alpha-D-mannose 1-phosphate > Pyrophosphate + Guanosine diphosphate mannose
Guanosine triphosphate + Molybdopterin > Pyrophosphate + Guanylyl molybdenum cofactor
Guanosine triphosphate + Inosinic acid + L-Aspartic acid > Guanosine diphosphate + Inorganic phosphate + N(6)-(1,2-dicarboxyethyl)AMP
Adenosine triphosphate + Guanosine triphosphate > Adenosine monophosphate + Guanosine 3'-diphosphate 5'-triphosphate
Guanosine triphosphate + 3 Water > Formic acid + 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Pyrophosphate
Adenosine triphosphate + Guanosine triphosphate > Adenosine monophosphate + Guanosine 3'-diphosphate 5'-triphosphate
2 Guanosine triphosphate >2 Pyrophosphate + Cyclic di-3',5'-guanylate
2 Guanosine triphosphate >2 Pyrophosphate + Cyclic di-3',5'-guanylate
2 Guanosine triphosphate >2 Pyrophosphate + Cyclic di-3',5'-guanylate
2 Guanosine triphosphate >2 Pyrophosphate + Cyclic di-3',5'-guanylate
2 Guanosine triphosphate >2 Pyrophosphate + Cyclic di-3',5'-guanylate
2 Guanosine triphosphate >2 Pyrophosphate + Cyclic di-3',5'-guanylate
2 Guanosine triphosphate >2 Pyrophosphate + Cyclic di-3',5'-guanylate
2 Guanosine triphosphate >2 Pyrophosphate + Cyclic di-3',5'-guanylate
Adenosine triphosphate + Guanosine triphosphate + Adenosyl cobinamide <> Adenosyl cobinamide phosphate + ADP + Guanosine diphosphate
Guanosine triphosphate + Water <> Formic acid + Dihydroneopterin triphosphate
Succinyl-CoA + Phosphate + Guanosine diphosphate + Succinyl-CoA <> Succinic acid + Coenzyme A + Guanosine triphosphate
Guanosine triphosphate + Inosinic acid + L-Aspartic acid + L-Aspartic acid > Guanosine diphosphate + Phosphate + N(6)-(1,2-dicarboxyethyl)AMP
Inosinic acid + L-Aspartic acid + Guanosine triphosphate + L-Aspartic acid > Guanosine diphosphate + Phosphate +2 Hydrogen ion + N(6)-(1,2-dicarboxyethyl)AMP + Adenylsuccinic acid
D-Mannose 1-phosphate + Guanosine triphosphate + Hydrogen ion > Pyrophosphate + Guanosine diphosphate mannose
α-D-mannose 1-phosphate + Guanosine triphosphate + Hydrogen ion > Guanosine diphosphate mannose + Pyrophosphate
Guanosine triphosphate + Water > Formic acid + Hydrogen ion + 7,8-dihydroneopterin 3'-triphosphate
Guanosine diphosphate + Adenosine triphosphate > Adenosine diphosphate + Guanosine triphosphate + ADP
Guanosine triphosphate + a reduced flavodoxin > dGTP + an oxidized flavodoxin + Water
adenosylcobinamide phosphate + Guanosine triphosphate + Hydrogen ion > Pyrophosphate + Adenosylcobinamide-GDP + Adenosylcobinamide-GDP
Guanosine triphosphate > Cyclic pyranopterin monophosphate + Pyrophosphate
Guanosine triphosphate + 3 Water > Formic acid + Pyrophosphate +2 Hydrogen ion + 2,5-Diamino-6-(5'-phosphoribosylamino)-4-pyrimidineone
Guanosine triphosphate + Water > 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Hydrogen ion + Formic acid + Pyrophosphate
Bis-molybdopterin guanine dinucleotide + Guanosine triphosphate + Hydrogen ion + Molybdopterin guanine dinucleotide > Guanylyl molybdenum cofactor + Pyrophosphate
More...

SMPDB Pathways:
Amino sugar and nucleotide sugar metabolism IIPW000887 Pw000887Pw000887 greyscalePw000887 simple
Aspartate metabolismPW000787 Pw000787Pw000787 greyscalePw000787 simple
Flavin biosynthesisPW001971 Pw001971Pw001971 greyscalePw001971 simple
Folate biosynthesisPW000908 Pw000908Pw000908 greyscalePw000908 simple
GTP degradationPW001888 Pw001888Pw001888 greyscalePw001888 simple
Mannose MetabolismPW000822 Pw000822Pw000822 greyscalePw000822 simple
Pyrimidine metabolismPW000942 Pw000942Pw000942 greyscalePw000942 simple
Tetrahydromonapterin BiosynthesisPW002043 Pw002043Pw002043 greyscalePw002043 simple
adenosylcobalamin salvage from cobinamidePW001884 Pw001884Pw001884 greyscalePw001884 simple
colanic acid building blocks biosynthesisPW000951 Pw000951Pw000951 greyscalePw000951 simple
guanylyl molybdenum cofactor biosynthesisPW002032 Pw002032Pw002032 greyscalePw002032 simple
preQ0 metabolismPW001893 Pw001893Pw001893 greyscalePw001893 simple
purine nucleotides de novo biosynthesisPW000910 Pw000910Pw000910 greyscalePw000910 simple
purine nucleotides de novo biosynthesis 1435709748PW000960 Pw000960Pw000960 greyscalePw000960 simple
purine nucleotides de novo biosynthesis 2PW002033 Pw002033Pw002033 greyscalePw002033 simple
KEGG Pathways:
EcoCyc Pathways:
Concentrations
ConcentrationStrainMediaGrowth StatusGrowth SystemTemperatureDetails
390± 24 uMK120.2 g/L NH4Cl, 2.0 g/L (NH4)2SO4, 3.25 g/L KH2PO4, 2.5 g/L K2HPO4, 1.5 g/L NaH2PO4, 0.5 g/L MgSO4; trace substances: 10 mg/L CaCl2, 0.5 mg/L ZnSO4, 0.25 mg/L CuCl2, 0.25 mg/L MnSO4, 0.175 mg/L CoCl2, 0.125 mg/L H3BO3, 2.5 mg/L AlCl3, 0.5 mg/L Na2MoO4, 10Stationary Phase, glucose limitedBioreactor, pH controlled, aerated, dilution rate=0.125 L/h37 oCPMID: 11488613
4870± 0 uMK12 NCM3722Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glucoseMid-Log PhaseShake flask and filter culture37 oCPMID: 19561621
2690± 0 uMK12 NCM3722Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glycerolMid-Log PhaseShake flask and filter culture37 oCPMID: 19561621
1250± 0 uMK12 NCM3722Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L acetateMid-Log PhaseShake flask and filter culture37 oCPMID: 19561621
589± 0 uMBW2511348 mM Na2HPO4, 22 mM KH2PO4, 10 mM NaCl, 45 mM (NH4)2SO4, supplemented with 1 mM MgSO4, 1 mg/l thiamine·HCl, 5.6 mg/l CaCl2, 8 mg/l FeCl3, 1 mg/l MnCl2·4H2O, 1.7 mg/l ZnCl2, 0.43 mg/l CuCl2·2H2O, 0.6 mg/l CoCl2·2H2O and 0.6 mg/l Na2MoO4·2H2O. 4 g/L GlucoStationary Phase, glucose limitedBioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h37 oCPMID: 17379776
Find out more about how we convert literature concentrations.
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
GC-MSGC-MS Spectrum - GC-MSsplash10-056v-8895330000-0a8a2d408be3cbe00023View in MoNA
GC-MSGC-MS Spectrum - GC-MS (2 TMS)splash10-0zos-8469026000-e08a35d5d35a9e63303cView in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-006t-0000970000-ed775d45b7d4c3b969dfView in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-0002-0000920000-eea0cfe4824f5aee7e4aView in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-0006-0900000000-895098906ea44c18ea43View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0udi-0911220000-75ec8e10f63e3aae4b1fView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0udi-0900000000-2b6055d302734ab3eecfView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0udi-0900000000-936551c9f8ce17b0cbfdView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0fk9-0730090000-511cdeecbbfb6b7c8615View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0zir-4930000000-cc969f818e5f659cd09cView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-004i-9300000000-dff84bbb768f44c2c74bView in MoNA
1D NMR1H NMR SpectrumNot Available
2D NMR[1H,13C] 2D NMR SpectrumNot Available
References
References:
  • Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. Pubmed: 19561621
  • Buchholz, A., Takors, R., Wandrey, C. (2001). "Quantification of intracellular metabolites in Escherichia coli K12 using liquid chromatographic-electrospray ionization tandem mass spectrometric techniques." Anal Biochem 295:129-137. Pubmed: 11488613
  • Chantin C, Bonin B, Boulieu R, Bory C: Liquid-chromatographic study of purine metabolism abnormalities in purine nucleoside phosphorylase deficiency. Clin Chem. 1996 Feb;42(2):326-8. Pubmed: 8595732
  • Chen Q, He Y, Yang K: Gene therapy for Parkinson's disease: progress and challenges. Curr Gene Ther. 2005 Feb;5(1):71-80. Pubmed: 15638712
  • Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597. Pubmed: 17379776
  • Iwanaga N, Yamamasu S, Tachibana D, Nishio J, Nakai Y, Shintaku H, Ishiko O: Activity of synthetic enzymes of tetrahydrobiopterin in the human placenta. Int J Mol Med. 2004 Jan;13(1):117-20. Pubmed: 14654981
  • Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. Pubmed: 22080510
  • Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. Pubmed: 21097882
  • Lester HA, Steer ML, Levitzki A: Prostaglandin-stimulated GTP hydrolysis associated with activation of adenylate cyclase in human platelet membranes. Proc Natl Acad Sci U S A. 1982 Feb;79(3):719-23. Pubmed: 6121325
  • Naylor EW, Ennis D, Davidson AG, Wong LT, Applegarth DA, Niederwieser A: Guanosine triphosphate cyclohydrolase I deficiency: early diagnosis by routine urine pteridine screening. Pediatrics. 1987 Mar;79(3):374-8. Pubmed: 3822637
  • Reichert LE Jr, Dattatreyamurty B: The follicle-stimulating hormone (FSH) receptor in testis: interaction with FSH, mechanism of signal transduction, and properties of the purified receptor. Biol Reprod. 1989 Jan;40(1):13-26. Pubmed: 2493820
  • Schmidt VA, Scudder L, Devoe CE, Bernards A, Cupit LD, Bahou WF: IQGAP2 functions as a GTP-dependent effector protein in thrombin-induced platelet cytoskeletal reorganization. Blood. 2003 Apr 15;101(8):3021-8. Epub 2002 Dec 19. Pubmed: 12515716
  • van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. Pubmed: 17765195
Synthesis Reference:Stiller, Regine; Thiem, Joachim. Preparative enzymatic conversion of guanosine-5'-monophosphate to guanosine-5'-triphosphate. Synlett (1990), (11), 709-10.
Material Safety Data Sheet (MSDS)Download (PDF)
External Links:
ResourceLink
CHEBI ID15996
HMDB IDHMDB01273
Pubchem Compound ID6830
Kegg IDC00044
ChemSpider ID6569
WikipediaGuanosine triphosphate
BioCyc IDGTP
EcoCyc IDGTP
Ligand ExpoGTP

Enzymes

General function:
Involved in adenylate cyclase activity
Specific function:
ATP = 3',5'-cyclic AMP + diphosphate
Gene Name:
cyaA
Uniprot ID:
P00936
Molecular weight:
97585
Reactions
ATP = 3',5'-cyclic AMP + diphosphate.
General function:
Involved in acid phosphatase activity
Specific function:
A phosphate monoester + H(2)O = an alcohol + phosphate
Gene Name:
appA
Uniprot ID:
P07102
Molecular weight:
47056
Reactions
A phosphate monoester + H(2)O = an alcohol + phosphate.
Myo-inositol hexakisphosphate + H(2)O = 1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate.
General function:
Involved in GTP cyclohydrolase I activity
Specific function:
GTP + H(2)O = formate + 2-amino-4-hydroxy-6- (erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
Gene Name:
folE
Uniprot ID:
P0A6T5
Molecular weight:
24830
Reactions
GTP + H(2)O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate.
General function:
Involved in nucleoside diphosphate kinase activity
Specific function:
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate
Gene Name:
ndk
Uniprot ID:
P0A763
Molecular weight:
15463
Reactions
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.
General function:
Involved in adenylosuccinate synthase activity
Specific function:
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP
Gene Name:
purA
Uniprot ID:
P0A7D4
Molecular weight:
47345
Reactions
GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP.
General function:
Involved in GTP cyclohydrolase II activity
Specific function:
Catalyzes the conversion of GTP to 2,5-diamino-6- ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate
Gene Name:
ribA
Uniprot ID:
P0A7I7
Molecular weight:
21836
Reactions
GTP + 3 H(2)O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate.
General function:
Involved in DNA-directed RNA polymerase activity
Specific function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme
Gene Name:
rpoA
Uniprot ID:
P0A7Z4
Molecular weight:
36511
Reactions
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
General function:
Involved in DNA-directed RNA polymerase activity
Specific function:
Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits
Gene Name:
rpoZ
Uniprot ID:
P0A800
Molecular weight:
10237
Reactions
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
General function:
Involved in ATP binding
Specific function:
ATP + uridine = ADP + UMP
Gene Name:
udk
Uniprot ID:
P0A8F4
Molecular weight:
24353
Reactions
ATP + uridine = ADP + UMP.
ATP + cytidine = ADP + CMP.
General function:
Involved in DNA binding
Specific function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Gene Name:
rpoC
Uniprot ID:
P0A8T7
Molecular weight:
155159
Reactions
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
General function:
Involved in DNA binding
Specific function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Gene Name:
rpoB
Uniprot ID:
P0A8V2
Molecular weight:
150631
Reactions
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
General function:
Involved in [formate-C-acetyltransferase]-activating enzyme activity
Specific function:
Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine
Gene Name:
nrdG
Uniprot ID:
P0A9N8
Molecular weight:
17446
General function:
Involved in magnesium ion binding
Specific function:
ATP + pyruvate = ADP + phosphoenolpyruvate
Gene Name:
pykF
Uniprot ID:
P0AD61
Molecular weight:
50729
Reactions
ATP + pyruvate = ADP + phosphoenolpyruvate.
General function:
Involved in nucleotide binding
Specific function:
ATP-dependent phosphorylation of adenosylcobinamide and adds GMP to adenosylcobinamide phosphate
Gene Name:
cobU
Uniprot ID:
P0AE76
Molecular weight:
20164
Reactions
ATP or GTP + adenosylcobinamide = adenosylcobinamide phosphate + ADP or GDP.
GTP + adenosylcobinamide phosphate = diphosphate + adenosylcobinamide-GDP.
General function:
Involved in nucleoside-triphosphate diphosphatase activity
Specific function:
Specific function unknown
Gene Name:
mazG
Uniprot ID:
P0AEY3
Molecular weight:
30412
Reactions
ATP + H(2)O = AMP + diphosphate.
General function:
Involved in amino acid binding
Specific function:
In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp
Gene Name:
relA
Uniprot ID:
P0AG20
Molecular weight:
83875
Reactions
ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate.
General function:
Involved in catalytic activity
Specific function:
In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes both the synthesis and degradation of ppGpp. The second messengers ppGpp and c-di-GMP together control biofilm formation in response to translational stress; ppGpp represses biofilm formation while c- di-GMP induces it
Gene Name:
spoT
Uniprot ID:
P0AG24
Molecular weight:
79342
Reactions
ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate.
Guanosine 3',5'-bis(diphosphate) + H(2)O = guanosine 5'-diphosphate + diphosphate.
General function:
Involved in magnesium ion binding
Specific function:
dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs
Gene Name:
dgt
Uniprot ID:
P15723
Molecular weight:
59382
Reactions
dGTP + H(2)O = deoxyguanosine + triphosphate.
General function:
Involved in catalytic activity
Specific function:
ATP + sulfate = diphosphate + adenylyl sulfate
Gene Name:
cysD
Uniprot ID:
P21156
Molecular weight:
35188
Reactions
ATP + sulfate = diphosphate + adenylyl sulfate.
General function:
Involved in magnesium ion binding
Specific function:
ATP + pyruvate = ADP + phosphoenolpyruvate
Gene Name:
pykA
Uniprot ID:
P21599
Molecular weight:
51357
Reactions
ATP + pyruvate = ADP + phosphoenolpyruvate.
General function:
Involved in GTPase activity
Specific function:
May be the GTPase, regulating ATP sulfurylase activity
Gene Name:
cysN
Uniprot ID:
P23845
Molecular weight:
52558
Reactions
ATP + sulfate = diphosphate + adenylyl sulfate.
General function:
Involved in nucleotidyltransferase activity
Specific function:
Involved in the biosynthesis of the capsular polysaccharide colanic acid
Gene Name:
manC
Uniprot ID:
P24174
Molecular weight:
53016
Reactions
GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose.
General function:
Involved in oxidoreductase activity
Specific function:
Transports electrons between flavodoxin or ferredoxin and NADPH. Involved in the reductive activation of cobalamin- independent methionine synthase, pyruvate formate lyase and anaerobic ribonucleotide reductase. Also protects against superoxide radicals due to methyl viologen in the presence of oxygen
Gene Name:
fpr
Uniprot ID:
P28861
Molecular weight:
27751
Reactions
2 reduced ferredoxin + NADP(+) + H(+) = 2 oxidized ferredoxin + NADPH.
General function:
Involved in catalytic activity
Specific function:
2'-deoxyribonucleoside triphosphate + thioredoxin disulfide + H(2)O = ribonucleoside triphosphate + thioredoxin
Gene Name:
nrdD
Uniprot ID:
P28903
Molecular weight:
80022
Reactions
2'-deoxyribonucleoside triphosphate + thioredoxin disulfide + H(2)O = ribonucleoside triphosphate + thioredoxin.
General function:
Involved in GTPase activity
Specific function:
May play a role in 30S ribosomal subunit biogenesis. Unusual circulary permuted GTPase that catalyzes rapid hydrolysis of GTP with a slow catalytic turnover. Dispensible for viability, but important for overall fitness. The intrinsic GTPase activity is stimulated by the presence of 30S (160-fold increase in kcat) or 70S (96 fold increase in kcat) ribosomes (PubMed:14973029). The GTPase is inhibited by aminoglycoside antibiotics such as neomycin and paromycin (PubMed:15466596) streptomycin and spectinomycin (PubMed:15828870). This inhibition is not due to competition for binding sites on the 30S or 70S ribosome (PubMed:15828870)
Gene Name:
rsgA
Uniprot ID:
P39286
Molecular weight:
39193
General function:
Involved in hydrolase activity
Specific function:
Hydrolyzes O6 atom-containing purine bases deoxyinosine triphosphate (dITP) and xanthosine triphosphate (XTP) as well as 2'-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) to nucleotide monophosphate and pyrophosphate. Probably excludes non- standard purines from DNA precursor pool, preventing thus incorporation into DNA and avoiding chromosomal lesions
Gene Name:
rdgB
Uniprot ID:
P52061
Molecular weight:
21039
Reactions
A nucleoside triphosphate + H(2)O = a nucleotide + diphosphate.
General function:
Involved in ATP binding
Specific function:
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. This small ubiquitous enzyme involved in the energy metabolism and nucleotide synthesis, is essential for maintenance and cell growth
Gene Name:
adk
Uniprot ID:
P69441
Molecular weight:
23586
Reactions
ATP + AMP = 2 ADP.
General function:
Involved in catalytic activity
Specific function:
Links a guanosine 5'-phosphate to molydopterin (MPT) forming molybdopterin guanine dinucleotide (MGD)
Gene Name:
mobA
Uniprot ID:
P32173
Molecular weight:
21643
Reactions
GTP + molybdenum cofactor = diphosphate + guanylyl molybdenum cofactor.
General function:
Involved in GTP binding
Specific function:
May bind the guanine nucleotide required for the synthesis of molybdopterin guanine dinucleotide
Gene Name:
mobB
Uniprot ID:
P32125
Molecular weight:
19363
General function:
Involved in FMN binding
Specific function:
Low-potential electron donor to a number of redox enzymes (Potential)
Gene Name:
fldB
Uniprot ID:
P0ABY4
Molecular weight:
19700
General function:
Involved in catalytic activity
Specific function:
Together with moaC, is involved in the conversion of a guanosine derivative (5'-GTP) into molybdopterin precursor Z
Gene Name:
moaA
Uniprot ID:
P30745
Molecular weight:
37346
General function:
Involved in FMN binding
Specific function:
Low-potential electron donor to a number of redox enzymes (Potential). Involved in the reactivation of inactive cob(II)alamin in methionine synthase
Gene Name:
fldA
Uniprot ID:
P61949
Molecular weight:
19737
General function:
Involved in Mo-molybdopterin cofactor biosynthetic process
Specific function:
Together with moaA, is involved in the conversion of a guanosine derivative (5'-GTP) into molybdopterin precursor Z
Gene Name:
moaC
Uniprot ID:
P0A738
Molecular weight:
17467
General function:
Replication, recombination and repair
Specific function:
Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions. MutT specifically degrades 8-oxo-dGTP to the monophosphate
Gene Name:
mutT
Uniprot ID:
P08337
Molecular weight:
14927
Reactions
8-oxo-dGTP + H(2)O = 8-oxo-dGMP + diphosphate.
General function:
Not Available
Specific function:
Not Available
Gene Name:
dosC
Uniprot ID:
P0AA89
Molecular weight:
Not Available
General function:
Not Available
Specific function:
Not Available
Gene Name:
yeaP
Uniprot ID:
P76245
Molecular weight:
Not Available
General function:
Signal transduction mechanisms
Specific function:
A probable diguanylate cyclase. The last member of a cascade of expressed proteins, its expression requires YdaM. AdrA production induces biosynthesis of cellulose in some E.coli isolates, but not in K12 strains. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria
Gene Name:
adrA
Uniprot ID:
P0AAP1
Molecular weight:
41537
Reactions
2 GTP = 2 diphosphate + cyclic di-3',5'-guanylate.

Transporters

General function:
Involved in nucleoside diphosphate kinase activity
Specific function:
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate
Gene Name:
ndk
Uniprot ID:
P0A763
Molecular weight:
15463
Reactions
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.
General function:
Involved in transporter activity
Specific function:
Non-specific porin
Gene Name:
ompN
Uniprot ID:
P77747
Molecular weight:
41220
General function:
Involved in transporter activity
Specific function:
Uptake of inorganic phosphate, phosphorylated compounds, and some other negatively charged solutes
Gene Name:
phoE
Uniprot ID:
P02932
Molecular weight:
38922
General function:
Involved in transporter activity
Specific function:
OmpF is a porin that forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane. It is also a receptor for the bacteriophage T2
Gene Name:
ompF
Uniprot ID:
P02931
Molecular weight:
39333
General function:
Involved in transporter activity
Specific function:
Forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane
Gene Name:
ompC
Uniprot ID:
P06996
Molecular weight:
40368