Escherichia coli K-12 substr. MG1655 Compound: GTP

Synonyms: guanylyl imidodiphosphate, guanosine 5'-triphosphate, guanosine-triphosphate

Superclasses: a nucleic acid component a nucleotide a nucleoside triphosphate a ribonucleoside triphosphate a purine ribonucleoside 5'-triphosphate
a nucleic acid component a nucleotide a purine nucleotide a purine ribonucleotide a purine ribonucleoside 5'-triphosphate
a nucleic acid component a nucleotide a ribonucleotide a purine ribonucleotide a purine ribonucleoside 5'-triphosphate
a nucleic acid component a nucleotide a ribonucleotide a ribonucleoside triphosphate a purine ribonucleoside 5'-triphosphate
a nucleic acid component
an organic heterocyclic compound an organic heterobicyclic compound a purine a purine nucleotide a purine ribonucleotide a purine ribonucleoside 5'-triphosphate
an organic heterocyclic compound an organonitrogen heterocyclic compound a purine a purine nucleotide a purine ribonucleotide a purine ribonucleoside 5'-triphosphate

Chemical Formula: C10H12N5O14P3

Molecular Weight: 519.15 Daltons

Monoisotopic Molecular Weight: 522.990659779 Daltons

GTP compound structure

SMILES: C(OP(=O)([O-])OP(=O)([O-])OP(=O)([O-])[O-])C1(OC(C(O)C(O)1)N3(C=NC2(C(=O)NC(N)=NC=23)))

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)/p-4/t3-,5-,6-,9-/m1/s1


Unification Links: CAS:86-01-1 , ChEBI:37565 , ChemSpider:5414499 , HMDB:HMDB01273 , IAF1260:33641 , KEGG:C00044 , MetaboLights:MTBLC37565 , PubChem:7058167

Standard Gibbs Free Energy of Change Formation (ΔfG in kcal/mol): -671.579

Reactions known to consume the compound:

6-hydroxymethyl-dihydropterin diphosphate biosynthesis I , preQ0 biosynthesis :
GTP + H2O → formate + 7,8-dihydroneopterin 3'-triphosphate + H+

adenosine ribonucleotides de novo biosynthesis :
L-aspartate + IMP + GTP → adenylo-succinate + GDP + phosphate + 2 H+

adenosylcobalamin salvage from cobinamide I :
adenosyl-cobinamide phosphate + GTP + H+ → adenosylcobinamide-GDP + diphosphate

flavin biosynthesis I (bacteria and plants) :
GTP + 3 H2O → 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + formate + diphosphate + 2 H+

GDP-mannose biosynthesis :
α-D-mannose 1-phosphate + GTP + H+ → GDP-α-D-mannose + diphosphate

guanosine deoxyribonucleotides de novo biosynthesis II :
dGTP + an oxidized flavodoxin + H2O ← GTP + a reduced flavodoxin

guanylyl molybdenum cofactor biosynthesis :
MoO2-molybdopterin cofactor + GTP + H+ → guanylyl molybdenum cofactor + diphosphate

molybdenum cofactor biosynthesis :
GTP → cyclic pyranopterin phosphate + diphosphate

ppGpp biosynthesis :
GTP + ATP → pppGpp + AMP

salvage pathways of pyrimidine ribonucleotides :
uridine + GTP → UMP + GDP + H+
cytidine + GTP → CMP + GDP + H+

Not in pathways:
GTP + 2 hydroxyl radical → 8-oxo-GTP + H2O
a 2-thiouridine34 in tRNA + a 5,10-methylene-tetrahydrofolate + ammonium + GTP + H2O → a 5-aminomethyl-2-thiouridine in tRNA + a 7,8-dihydrofolate + GDP + phosphate
an RNA terminal-2',3'-cyclic-phosphate + a 5'-hydroxyl terminated RNA + GTP → a ligated RNA + GMP + diphosphate
GTP + H2O → GDP + phosphate + H+
2 GTP → cyclic di-3',5'-guanylate + 2 diphosphate

Not in pathways:
a nucleoside triphosphate + H2O → a nucleoside 5'-monophosphate + diphosphate + H+

Reactions known to produce the compound:

guanosine ribonucleotides de novo biosynthesis :

ppGpp biosynthesis :
pppGpp + H2O → GTP + diphosphate + H+

Not in pathways:
a nucleoside diphosphate + ATP → a nucleoside triphosphate + ADP

Reactions known to both consume and produce the compound:

Not in pathways:
GTP ↔ cyclic-GMP + diphosphate

In Reactions of unknown directionality:

Not in pathways:
a 2-thiouridine34 in tRNA + GTP + glycine + a 5,10-methylene-tetrahydrofolate + H2O = a 5-carboxymethylaminomethyl-2-thiouridine in tRNA + GDP + a 7,8-dihydrofolate + phosphate
a uridine34 in tRNA + GTP + a 5,10-methylene-tetrahydrofolate + glycine + H2O = a 5-carboxymethylaminomethyluridine in tRNA + GDP + a 7,8-dihydrofolate + phosphate

Not in pathways:
a reduced flavodoxin + a ribonucleoside triphosphate = an oxidized flavodoxin + a deoxyribonucleoside triphosphate + H2O

Not in pathways:
a nucleoside triphosphate + RNA(n) = RNA(n+1) + diphosphate

Enzymes activated by GTP, sorted by the type of activation, are:

Activator (Allosteric) of: thymidine kinase [Iwatsuki67, Chen78] , phosphoenolpyruvate carboxylase [Izui81] , UMP kinase [Serina95, Meyer08] , CTP synthase [Levitzki72, Comment 1]

Activator (Mechanism unknown) of: ornithine decarboxylase [Kanjee11] , amidophosphoribosyl transferase [Messenger79] , ornithine decarboxylase [Comment 2] , uracil phosphoribosyltransferase [Rasmussen86]

Enzymes inhibited by GTP, sorted by the type of inhibition, are:

Inhibitor (Competitive) of: guanosine kinase [Comment 3] , nucleoside diphosphate kinase [Roisin78, Comment 4] , guanylate kinase [Oeschger66, Comment 5] , deoxyguanosine triphosphate triphosphohydrolase [Kornberg58] , ITPase [Zheng05]

Inhibitor (Noncompetitive) of: phosphoglucomutase [Duckworth73, Sanwal72] , adenylate cyclase [Yang83]

Inhibitor (Mechanism unknown) of: m7GTP pyrophosphatase [Tchigvintsev13] , thiamine phosphate synthase [Kayama73, Kawasaki79] , nucleoside diphosphate kinase [Roisin78, Comment 6] , methylenetetrahydrofolate dehydrogenase [Dev78]

This compound has been characterized as a cofactor or prosthetic group of the following enzymes: McrBC restriction endonuclease

This compound has been characterized as an alternative substrate of the following enzymes: adenylate kinase , tRNAMet cytidine acetyltransferase , guanylate kinase , hydroxymethylpyrimidine kinase , deoxyguanosine triphosphate triphosphohydrolase , tetraacyldisaccharide 4'-kinase , NAD kinase , nucleoside di- and triphosphate hydrolase , ATP synthase , thymidine kinase , xanthosine triphosphate pyrophosphatase , CMP kinase , ATPase , RNA 3'-terminal phosphate cyclase , adenylate cyclase , pantothenate kinase , succinyl-CoA synthetase , 1-phosphofructokinase , folylpoly-γ-glutamate synthetase


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Chen78: Chen MS, Prusoff WH (1978). "Thymidine kinase from Escherichia coli." Methods Enzymol 1978;51;354-60. PMID: 357898

Dev78: Dev IK, Harvey RJ (1978). "A complex of N5,N10-methylenetetrahydrofolate dehydrogenase and N5,N10-methenyltetrahydrofolate cyclohydrolase in Escherichia coli. Purification, subunit structure, and allosteric inhibition by N10-formyltetrahydrofolate." J Biol Chem 1978;253(12);4245-53. PMID: 350870

Duckworth73: Duckworth HW, Barber BH, Sanwal BD (1973). "The interaction of phosphoglucomutase with nucleotide inhibitors." J Biol Chem 248(4);1431-5. PMID: 4568817

Iwatsuki67: Iwatsuki N, Okazaki R (1967). "Mechanism of regulation of deoxythymidine kinase of Escherichia coli. I. Effect of regulatory deoxynucleotides on the state of aggregation of the enzyme." J Mol Biol 1967;29(1);139-54. PMID: 4861610

Izui81: Izui K, Taguchi M, Morikawa M, Katsuki H (1981). "Regulation of Escherichia coli phosphoenolpyruvate carboxylase by multiple effectors in vivo. II. Kinetic studies with a reaction system containing physiological concentrations of ligands." J Biochem 90(5);1321-31. PMID: 7040354

Kanjee11: Kanjee U, Gutsche I, Ramachandran S, Houry WA (2011). "The Enzymatic Activities of the Escherichia coli Basic Aliphatic Amino Acid Decarboxylases Exhibit a pH Zone of Inhibition." Biochemistry 50(43);9388-98. PMID: 21957966

Kawasaki00: Kawasaki H, Shimaoka M, Usuda Y, Utagawa T (2000). "End-product regulation and kinetic mechanism of guanosine-inosine kinase from Escherichia coli." Biosci Biotechnol Biochem 2000;64(5);972-9. PMID: 10879466

Kawasaki79: Kawasaki T (1979). "Thiamine phosphate pyrophosphorylase." Methods Enzymol 1979;62;69-73. PMID: 374983

Kayama73: Kayama Y, Kawasaki T (1973). "Purification and properties of thiaminephosphate pyrophosphorylase of Escherichia coli." Arch Biochem Biophys 1973;158(1);242-8. PMID: 4580841

Kornberg58: Kornberg SR, Lehman IR, Bessman MJ, Simms ES, Kornberg A (1958). "Enzymatic cleavage of deoxyguanosine triphosphate to deoxyguanosine and tripolyphosphate." J Biol Chem 1958; 233:159-162. PMID: 13563461

Koshland74: Koshland DE, Levitzki A "CTP Synthetase and Related Enzymes." Academic Press, New York 1974;3:539-559.

Levitzki72: Levitzki A, Koshland DE (1972). "Role of an allosteric effector. Guanosine triphosphate activation in cytosine triphosphate synthetase." Biochemistry 11(2);241-6. PMID: 4550559

Messenger79: Messenger LJ, Zalkin H (1979). "Glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli. Purification and properties." J Biol Chem 1979;254(9);3382-92. PMID: 372191

Meyer08: Meyer P, Evrin C, Briozzo P, Joly N, Barzu O, Gilles AM (2008). "Structural and functional characterization of Escherichia coli UMP kinase in complex with its allosteric regulator GTP." J Biol Chem 283(51);36011-8. PMID: 18945668

Oeschger66: Oeschger MP, Bessman MJ (1966). "Purification and properties of guanylate kinase from Escherichia coli." J Biol Chem 1966;241(22);5452-60. PMID: 5333666

Rasmussen86: Rasmussen UB, Mygind B, Nygaard P (1986). "Purification and some properties of uracil phosphoribosyltransferase from Escherichia coli K12." Biochim Biophys Acta 1986;881(2);268-75. PMID: 3513846

Roisin78: Roisin MP, Kepes A (1978). "Nucleosidediphosphate kinase of Escherichia coli, a periplasmic enzyme." Biochim Biophys Acta 1978;526(2);418-28. PMID: 214126

Sanwal72: Sanwal BD, Duckworth HW, Hollier ML (1972). "Regulation of phosphoglucomutase." Biochem J 128(1);26P-27P. PMID: 4563765

Serina95: Serina L, Blondin C, Krin E, Sismeiro O, Danchin A, Sakamoto H, Gilles AM, Barzu O (1995). "Escherichia coli UMP-kinase, a member of the aspartokinase family, is a hexamer regulated by guanine nucleotides and UTP." Biochemistry 1995;34(15);5066-74. PMID: 7711027

Tchigvintsev13: Tchigvintsev A, Tchigvintsev D, Flick R, Popovic A, Dong A, Xu X, Brown G, Lu W, Wu H, Cui H, Dombrowski L, Joo JC, Beloglazova N, Min J, Savchenko A, Caudy AA, Rabinowitz JD, Murzin AG, Yakunin AF (2013). "Biochemical and structural studies of conserved maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides." Chem Biol 20(11);1386-98. PMID: 24210219

Weng86: Weng M, Makaroff CA, Zalkin H (1986). "Nucleotide sequence of Escherichia coli pyrG encoding CTP synthetase." J Biol Chem 1986;261(12);5568-74. PMID: 3514618

Yang83: Yang JK, Epstein W (1983). "Purification and characterization of adenylate cyclase from Escherichia coli K12." J Biol Chem 1983;258(6);3750-8. PMID: 6300054

Zheng05: Zheng J, Singh VK, Jia Z (2005). "Identification of an ITPase/XTPase in Escherichia coli by structural and biochemical analysis." Structure 13(10);1511-20. PMID: 16216582

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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