2'-Deoxyguanosine 5'-monophosphate (PAMDB000231)

IdentificationTaxonomyPhysical PropertiesBiological PropertiesSpectraConcentrationsLinksReferencesEnzymes Transporters
Proteins (3280)
Record Information
Version 1.0
Update Date 1/22/2018 11:54:54 AM
Metabolite IDPAMDB000231
Identification
Name: 2'-Deoxyguanosine 5'-monophosphate
Description:2'-Deoxyguanosine 5'-monophosphate is a derivative of the common nucleic acid GTP, or guanosine triphosphate, in which the -OH (hydroxyl) group on the 2' carbon on the nucleotide's pentose has been removed (hence the deoxy- part of the name). Additionally, the diphosphate of the name indicates that two of the phosphoryl groups of GTP have been removed, most likely by hydrolysis (Wikipedia).
Structure
Thumb
🔍MOLSDFPDBSMILESInChIView Structure
Synonyms:
  • 2'-Deoxy-5'-GMP
  • 2'-Deoxy-5'-guanylate
  • 2'-Deoxy-5'-guanylic acid
  • 2'-Deoxy-GMP
  • 2'-Deoxy-Guanosine 5'-(dihydrogen phosphate)
  • 2'-Deoxy-guanosine 5'-(dihydrogen phosphoric acid)
  • 2'-Deoxy-Guanosine 5'-phosphate
  • 2'-Deoxy-guanosine 5'-phosphoric acid
  • 2'-Deoxy-Guanosine phosphate
  • 2'-Deoxy-guanosine phosphoric acid
  • 2'-Deoxyguanosine 5'-monophosphate
  • 2'-Deoxyguanosine 5'-monophosphoric acid
  • 2'-Deoxyguanosine 5'-phosphate
  • 2'-Deoxyguanosine 5'-phosphoric acid
  • 2'-Deoxyguanosine-5'-phosphate
  • 2'-Deoxyguanosine-5'-phosphoric acid
  • 2'-Deoxyguanylate
  • 2'-Deoxyguanylic acid
  • 2'-DG-5'-MP
  • 2'-dGMP
  • Deoxy-GMP
  • Deoxyguanosine 5'-monophosphate
  • Deoxyguanosine 5'-monophosphoric acid
  • Deoxyguanosine 5'-phosphate
  • Deoxyguanosine 5'-phosphoric acid
  • Deoxyguanosine-phosphate
  • Deoxyguanosine-phosphoric acid
  • DGMP
  • G
  • Guanine riboside
  • Vernine
Chemical Formula: C10H14N5O7P
Average Molecular Weight: 347.2212
Monoisotopic Molecular Weight: 347.063084339
InChI Key: LTFMZDNNPPEQNG-KVQBGUIXSA-N
InChI:InChI=1S/C10H14N5O7P/c11-10-13-8-7(9(17)14-10)12-3-15(8)6-1-4(16)5(22-6)2-21-23(18,19)20/h3-6,16H,1-2H2,(H2,18,19,20)(H3,11,13,14,17)/t4-,5+,6+/m0/s1
CAS number: 902-04-5
IUPAC Name:{[(2R,3S,5R)-5-(2-amino-6-oxo-6,9-dihydro-3H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy}phosphonic acid
Traditional IUPAC Name: deoxyguanylate
SMILES:NC1=NC(=O)C2=C(N1)N(C=N2)[C@H]1C[C@H](O)[C@@H](COP(O)(O)=O)O1
Chemical Taxonomy
Taxonomy DescriptionThis compound belongs to the class of organic compounds known as purine ribonucleoside monophosphates. These are nucleotides consisting of a purine base linked to a ribose to which one monophosphate group is attached.
Kingdom Organic compounds
Super ClassNucleosides, nucleotides, and analogues
Class Purine nucleotides
Sub ClassPurine ribonucleotides
Direct Parent Purine ribonucleoside monophosphates
Alternative Parents
Substituents
  • Purine ribonucleoside monophosphate
  • Hypoxanthine
  • 6-oxopurine
  • Purine
  • Imidazopyrimidine
  • Monoalkyl phosphate
  • Pyrimidone
  • Alkyl phosphate
  • Pyrimidine
  • Primary aromatic amine
  • Phosphoric acid ester
  • Organic phosphoric acid derivative
  • Organic phosphate
  • N-substituted imidazole
  • Saccharide
  • Heteroaromatic compound
  • Vinylogous amide
  • Oxolane
  • Imidazole
  • Azole
  • Secondary alcohol
  • Lactam
  • Oxacycle
  • Azacycle
  • Organoheterocyclic compound
  • Hydrocarbon derivative
  • Primary amine
  • Organooxygen compound
  • Organonitrogen compound
  • Amine
  • Alcohol
  • Aromatic heteropolycyclic compound
Molecular Framework Aromatic heteropolycyclic compounds
External Descriptors
Physical Properties
State: Solid
Charge:-2
Melting point: Not Available
Experimental Properties:
PropertyValueSource
Predicted Properties
PropertyValueSource
Water Solubility2.67 mg/mLALOGPS
logP-1.9ALOGPS
logP-2.8ChemAxon
logS-2.1ALOGPS
pKa (Strongest Acidic)1.21ChemAxon
pKa (Strongest Basic)2.62ChemAxon
Physiological Charge-2ChemAxon
Hydrogen Acceptor Count10ChemAxon
Hydrogen Donor Count5ChemAxon
Polar Surface Area181.52 Å2ChemAxon
Rotatable Bond Count4ChemAxon
Refractivity73.55 m3·mol-1ChemAxon
Polarizability29.86 Å3ChemAxon
Number of Rings3ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations: Cytoplasm
Reactions:
dGTP + Water > 2'-Deoxyguanosine 5'-monophosphate + Hydrogen ion + Pyrophosphate
2'-Deoxyguanosine 5'-monophosphate + Water > Deoxyguanosine + Phosphate
Adenosine triphosphate + 2'-Deoxyguanosine 5'-monophosphate <> ADP + dGDP
dGTP + Water <> 2'-Deoxyguanosine 5'-monophosphate + Pyrophosphate
Adenosine triphosphate + 2'-Deoxyguanosine 5'-monophosphate <> ADP + dGDP
Pathways:
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-0fr2-0598000000-21b063e2aff7146d8568View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF (UPLC Q-Tof Premier, Waters) , Positivesplash10-0udi-0900000000-d2858e957ac8a4c91e79View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF (UPLC Q-Tof Premier, Waters) , Negativesplash10-004j-9203000000-40bcf8d5e1ae6813c4f7View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, NegativeNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, NegativeNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, NegativeNot Available
1D NMR1H NMR SpectrumNot Available
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
  • 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
  • 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
  • Warnecke A, Fichtner I, Garmann D, Jaehde U, Kratz F: Synthesis and biological activity of water-soluble maleimide derivatives of the anticancer drug carboplatin designed as albumin-binding prodrugs. Bioconjug Chem. 2004 Nov-Dec;15(6):1349-59. Pubmed: 15546202
Synthesis Reference: Reichard, Peter. Formation of deoxyguanosine 5'-phosphate from guanosine 5'-phosphate with enzymes from chick embryos. Biochimica et Biophysica Acta (1960), 41 368-9.
Material Safety Data Sheet (MSDS) Download (PDF)
External Links:
ResourceLink
CHEBI ID16192
HMDB IDHMDB01044
Pubchem Compound ID65059
Kegg IDC00362
ChemSpider ID58570
Wikipedia IDNot Available
BioCyc IDDGMP
EcoCyc IDDGMP
Ligand ExpoPG7

Enzymes

Protein Details
• Multifunctional protein surE
General function:
Involved in hydrolase activity
Specific function:
Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'- monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain- length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. Also plays a significant physiological role in stress-response and is required for the survival of Pseudomonas aeruginosa in stationary growth phase
Gene Name:
surE
Locus Tag:
PA3625
Molecular weight:
26.4 kDa
Reactions
A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate.
A 3'-ribonucleotide + H(2)O = a ribonucleoside + phosphate.
(Polyphosphate)(n) + H(2)O = (polyphosphate)(n-1) + phosphate.
Protein Details
• Class B acid phosphatase
General function:
Involved in acid phosphatase activity
Specific function:
Dephosphorylates several organic phosphomonoesters and catalyzes the transfer of low-energy phosphate groups from phosphomonoesters to hydroxyl groups of various organic compounds. Preferentially acts on aryl phosphoesters. Might function as a broad-spectrum dephosphorylating enzyme able to scavenge both 3'- and 5'-nucleotides and also additional organic phosphomonoesters
Gene Name:
aphA
Locus Tag:
PA1409
Molecular weight:
38 kDa
Reactions
A phosphate monoester + H(2)O = an alcohol + phosphate.
Protein Details
• Protein mazG
General function:
Involved in nucleoside-triphosphate diphosphatase activity
Specific function:
Specific function unknown
Gene Name:
mazG
Locus Tag:
PA0935
Molecular weight:
31.2 kDa
Reactions
ATP + H(2)O = AMP + diphosphate.
Protein Details
• Nucleoside-triphosphatase rdgB
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
Locus Tag:
PA0387
Molecular weight:
21.2 kDa
Reactions
A nucleoside triphosphate + H(2)O = a nucleotide + diphosphate.
Protein Details
• Guanylate kinase
General function:
Involved in protein binding
Specific function:
Essential for recycling GMP and indirectly, cGMP
Gene Name:
gmk
Locus Tag:
PA5336
Molecular weight:
23.1 kDa
Reactions
ATP + GMP = ADP + GDP.
Protein Details
• Mutator mutT protein
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
Locus Tag:
PA4400
Molecular weight:
34 kDa
Reactions
8-oxo-dGTP + H(2)O = 8-oxo-dGMP + diphosphate.

Transporters