|
|
| guanosine 5'-monophosphate |
|
| CHEBI:17345 |
|
| A purine ribonucleoside 5'-monophosphate having guanine as the nucleobase. |
|
This entity has been manually annotated by the ChEBI Team.
|
|
|
CHEBI:40119, CHEBI:42979, CHEBI:42831, CHEBI:42615, CHEBI:42887, CHEBI:42892, CHEBI:42647, CHEBI:47450, CHEBI:5228, CHEBI:13341, CHEBI:14381, CHEBI:24449, CHEBI:24450, CHEBI:29058
|
|
| ChemicalBook:CB6271952, eMolecules:29480205, eMolecules:5747772, ZINC000002159505 |
|
|
Molfile
XML
SDF
|
|
|
more structures >>
|
|
call loadScript javascripts\jsmol\core\package.js call loadScript javascripts\jsmol\core\core.z.js -- required by ClazzNode call loadScript javascripts\jsmol\J\awtjs2d\WebOutputChannel.js
|
| Guanosine monophosphate (GMP), also known as 5′-guanidylic acid or guanylic acid (conjugate base guanylate), is a nucleotide that is used as a monomer in RNA. It is an ester of phosphoric acid with the nucleoside guanosine. GMP consists of the phosphate group, the pentose sugar ribose, and the nucleobase guanine; hence it is a ribonucleotide monophosphate. Guanosine monophosphate is commercially produced by microbial fermentation.
As an acyl substituent, it takes the form of the prefix guanylyl-. |
|
Read full article at Wikipedia
|
InChI=1S/C10H14N5O8P/c11- 10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(23-9)1-22-24(19,20)21/h2-3,5-6,9,16-17H,1H2,(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1 |
| RQFCJASXJCIDSX-UUOKFMHZSA-N |
| Nc1nc2n(cnc2c(=O)[nH]1)[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]1O |
|
|
Mus musculus
(NCBI:txid10090)
|
Source: BioModels - MODEL1507180067
See:
PubMed
|
|
Escherichia coli
(NCBI:txid562)
|
See:
PubMed
|
|
Escherichia coli metabolite
Any bacterial metabolite produced during a metabolic reaction in Escherichia coli.
mouse metabolite
Any mammalian metabolite produced during a metabolic reaction in a mouse (Mus musculus).
metabolite
Any intermediate or product resulting from metabolism. The term 'metabolite' subsumes the classes commonly known as primary and secondary metabolites.
|
|
|
biomarker
A substance used as an indicator of a biological state.
|
|
View more via ChEBI Ontology
|
5'-guanylic acid
|
|
[(2R,3S,4R,5R)-5-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen phosphate
|
|
5'-GMP
|
ChemIDplus
|
|
GMP
|
KEGG COMPOUND
|
|
Guanosine 5'-monophosphate
|
KEGG COMPOUND
|
|
Guanosine 5'-phosphate
|
KEGG COMPOUND
|
|
Guanosine monophosphate
|
KEGG COMPOUND
|
|
guanosine-5'-monophosphate
|
PDBeChem
|
|
Guanylic acid
|
KEGG COMPOUND
|
|
pG
|
ChEBI
|
|
59430
|
Reaxys Registry Number
|
Reaxys
|
|
85-32-5
|
CAS Registry Number
|
ChemIDplus
|
Bordbar A, Mo ML, Nakayasu ES, Schrimpe-Rutledge AC, Kim YM, Metz TO, Jones MB, Frank BC, Smith RD, Peterson SN, Hyduke DR, Adkins JN, Palsson BO (2012)
Model-driven multi-omic data analysis elucidates metabolic immunomodulators of macrophage activation.
Molecular systems biology 8, 558 [PubMed:22735334]
[show Abstract]
Macrophages are central players in immune response, manifesting divergent phenotypes to control inflammation and innate immunity through release of cytokines and other signaling factors. Recently, the focus on metabolism has been reemphasized as critical signaling and regulatory pathways of human pathophysiology, ranging from cancer to aging, often converge on metabolic responses. Here, we used genome-scale modeling and multi-omics (transcriptomics, proteomics, and metabolomics) analysis to assess metabolic features that are critical for macrophage activation. We constructed a genome-scale metabolic network for the RAW 264.7 cell line to determine metabolic modulators of activation. Metabolites well-known to be associated with immunoactivation (glucose and arginine) and immunosuppression (tryptophan and vitamin D3) were among the most critical effectors. Intracellular metabolic mechanisms were assessed, identifying a suppressive role for de-novo nucleotide synthesis. Finally, underlying metabolic mechanisms of macrophage activation are identified by analyzing multi-omic data obtained from LPS-stimulated RAW cells in the context of our flux-based predictions. Our study demonstrates metabolism's role in regulating activation may be greater than previously anticipated and elucidates underlying connections between activation and metabolic effectors. | Yashima Y, Ohgane T (2001)
[Pharmacological profiles of mycophenolate mofetil (CellCept), a new immunosuppressive agent].
Nihon yakurigaku zasshi. Folia pharmacologica Japonica 117, 131-137 [PubMed:11233304]
[show Abstract]
Mycophenolate mofetil (MMF, CellCept), a semisynthetic derivative of mycophenolic acid (MPA) produced by a fungus, is an inhibitor of the inosine monophosphate dehydrogenase (IMPDH) enzyme (IC50 = 25 nM) that catalyzes the synthesis of guanosine monophosphate (GMP) from inosine. GMP is an essential nucleoside for purine synthesis during cell division. As T and B-lymphocytes almost exclusively use the de novo pathway of purine synthesis, these cells are particularly sensitive to the inhibitory action of MMF. It has a mechanism of action distinct from cyclosporine and tacrolimus. Although MMF does not affect cytokine production, by inhibiting the rate-limiting enzyme IMPDH in the de novo synthesis of purines, it inhibits the proliferation of T and B-lymphocytes, the production of antibodies, and the generation of cytotoxic T lymphocytes. Reversal of acute allograft rejection and increased survival of kidney, heart and bone marrow cell allograft has been shown in several animal studies. Moreover, it was suggested that MMF combined with CsA prevented the acute rejection, and approximately half of the animals became long-term survivors. The Ministry of Health and Welfare approved MMF in 1999 for use for rejection treatment in renal transplantation based on several prospective, randomized and blind efficacy trials. | Choi S, Mahalingaiah S, Delaney S, Neale NR, Masood S (1999)
Substitution and Reduction of Platinum(IV) Complexes by a Nucleotide, Guanosine 5'-Monophosphate.
Inorganic chemistry 38, 1800-1805 [PubMed:11670950]
[show Abstract]
A series of Pt(IV) anticancer complexes with different reduction potentials has been investigated for their reactivity toward 5'-guanosine monophosphate (5'-GMP). The Pt(IV) complexes studied were Pt(IV)(trans-d,l)(1,2-(NH(2))(2)C(6)H(10))Cl(4) (tetraplatin, Pt(IV)(dach)Cl(4); dach = diaminocyclohexane), cis,trans,cis-[Pt(IV)((CH(3))(2)CHNH(2))(2)(OH)(2)Cl(2)] (iproplatin, Pt(IV)(ipa)(2)(OH)(2)Cl(2); ipa = isopropylamine), cis,trans,cis-[Pt(IV)(en)(OH)(2)Cl(2)] (Pt(IV)(en)(OH)(2)Cl(2); en = ethylenediamine), Pt(IV)(en)Cl(4), and cis,trans,cis-[Pt(IV)(en)(OCOCH(3))(2)Cl(2)] (Pt(IV)(en)(OCOCH(3))(2)Cl(2)). The reactivity was monitored by the decreased (1)H NMR peak intensity at 8.2 ppm due to H8 of free 5'-GMP and the increased intensity of a new peak around 8.6 ppm due to H8 of 5'-GMP bound to Pt(II). The reactivity followed the order of cathodic reduction potentials of the Pt(IV) complexes: Pt(IV)(dach)Cl(4) (-90 mV) >> Pt(IV)(en)Cl(4) (-160 mV) > Pt(IV)(en)(OCOCH(3))(2)Cl(2) (-546 mV) > Pt(IV)(ipa)(2)(OH)(2)Cl(2) (-730 mV). The most reactive complex, Pt(IV)(dach)Cl(4), showed an additional weak peak at 9.2 ppm due to H8 of the 5'-GMP bound to the Pt(IV) complex, indicating the existence of a Pt(IV) intermediate. (1)H NMR, UV/visible absorption spectra, and high-performance liquid chromatograms suggest that the final product is Pt(II)(dach)(5'-GMP)(ox5'-GMP), where ox5'-GMP is oxidized 5'-GMP. A plausible mechanism is that there is an initial substitution of one Pt(IV)/ligand by a 5'-GMP molecule, followed by a two-electron reduction, and finally a second substitution by another 5'-GMP. In the presence of excess 5'-GMP (at least 20-fold), ox5'-GMP seems to be replaced by 5'-GMP to form Pt(II)(dach)(5'-GMP)(2). UV/visible absorption spectroscopy shows that the formation of the Pt(IV) intermediate by substitution is a very slow process followed by reduction. The reduction is characterized by a relatively fast exponential decay. The addition of a small amount of cis-[Pt(II)(NH(3))(2)Cl(2)] shortened the slow formation time of the intermediate, implicating the occurrence of a Pt(II)-assisted substitution reaction. These reactions may lead to a better understanding of the anticancer activity of Pt(IV) complexes. | Munns TW, Freeman SK (1989)
Antibody-nucleic acid complexes. Oligo(dG)n and -(dT)n specificities associated with anti-DNA antibodies from autoimmune MRL mice.
Biochemistry 28, 10048-10054 [PubMed:2559771]
[show Abstract]
The specificity of anti-DNA antibodies in the sera of unimmunized autoimmune MRL mice was initially assessed via an enzyme-linked immunosorbent assay (ELISA). Antibody binding profiles to a panel of immobilized antigens (AMP-, GMP-, CMP-, UMP-, and TMP-BSA, ss- and dsDNA) demonstrated high levels of immunoglobulins reacting with GMP and ssDNA and intermediate levels with AMP, TMP, and dsDNA. Fractionation of serum anti-DNA antibodies into subsets on the basis of their binding to GMP- and TMP-agarose indicated that the resulting GMP- or TMP-reactive antibodies bound to their homologous nucleotides and ssDNA. Competition-inhibition studies with soluble mono-, oligo-, and polynucleotides revealed that GMP- and TMP-reactive antibodies were highly specific for oligo(dG)n and -(dT)n sequences, respectively. Whereas the relative affinity of TMP-reactive autoantibodies to oligo(dT)n increased with oligonucleotide length (n = 2, 4, 6, 8, 10, 15), GMP-reactive antibodies preferentially recognized oligo(dG)10 (Ka congruent to 1 x 10(7) M-1). While neither antibody recognized oligo(dA)8 and -(dC)8 competitors, mixed-base oligonucleotides were inhibitory at concentrations approximately 10-fold greater than similarly sized oligo(dG)n and -(dT)n sequences. Similar characterizations of both pooled and individual MRL sera indicated that anti-DNA antibodies represent 8-10% of the total serum IgG. More importantly, GMP-reactive autoantibodies predominated and accounted for 60-70% of the entire unbound anti-DNA antibody population. | Zouali M, Migliorini P, Stollar DB (1987)
Murine lupus anti-DNA antibodies cross-react with the hapten (4-hydroxy-5-iodo-3-nitrophenyl)acetyl, but immunization-induced anti-DNA antibodies do not.
European journal of immunology 17, 509-513 [PubMed:3569407]
[show Abstract]
The antigen-binding selectivity of 2 sets of anti-DNA antibodies from autoimmune mice and from normal mice was examined. Eighteen affinity-purified anti-DNA auto-antibodies from MRL-lpr/lpr mice were examined for binding to the haptens azobenzenearsonate, phosphorylcholine, (4-hydroxy-3-nitrophenyl)acetyl and (4-hydroxy-5-iodo-3-nitrophenyl)acetyl (NIP). Five of these autoantibodies bound to NIP-protein conjugates. In contrast, none of 12 monoclonal antibodies to single-stranded DNA or left-handed Z-DNA induced by immunization of BALB/c and C57BL/6 mice with nucleic acid antigens reacted with the tested haptens. In a reciprocal test of the relationship between anti-DNA and anti-NIP binding, we examined 24 monoclonal antibodies to NIP, from various strains of mice, for binding to DNA. One such antibody from a BALB/c mouse also bound to DNA. These results are discussed in the context of the mechanisms underlying autoantibody hyperproduction. |
|
