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Identification
YMDB IDYMDB00700
NamedATP
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionDeoxyadenosine triphosphate (dATP) is a nucleotide used in cells for DNA synthesis. DNA usually exists as a double-stranded structure, with both strands coiled together to form the characteristic double-helix. Each single strand of DNA is a chain of four types of nucleotides having the bases: adenine, cytosine, guanine, and thymine. A nucleotide is a mono-, di-, or triphosphate deoxyribonucleoside; that is, a deoxyribose sugar is attached to one, two, or three phosphates. Chemical interaction of these nucleotides forms phosphodiester linkages, creating the phosphate-deoxyribose backbone of the DNA double helix with the bases pointing inward. Nucleotides (bases) are matched between strands through hydrogen bonds to form base pairs. Adenine pairs with thymine, and cytosine pairs with guanine. [Wikipedia]
Structure
Thumb
Synonyms
  • 2-deoxyadenosine 5-triphosphate
  • 2'-Deoxy-5'-ATP
  • 2'-Deoxy-ATP
  • 2'-Deoxyadenosine 5'-triphosphate
  • 2'-deoxyadenosine triphosphate
  • dATP
  • Deoxy-ATP
  • deoxyadenosine 5-triphosphate
  • Deoxyadenosine 5'-triphosphate
  • deoxyadenosine triphosphate
  • deoxyadenosine-triphosphate
  • DTP
  • 2'-Deoxyadenosine 5'-triphosphoric acid
  • Deoxyadenosine 5'-triphosphoric acid
  • Deoxyadenosine triphosphoric acid
  • 2'-Deoxyadenosine triphosphate, 14C-labeled
  • 2'-Deoxyadenosine triphosphate, monomagnesium salt
  • 2'-Deoxyadenosine triphosphate, trisodium salt
  • 2'-Deoxyadenosine triphosphate, p'-(32)p-labeled
  • dATP CPD
CAS number1927-31-7
WeightAverage: 491.1816
Monoisotopic: 491.000830537
InChI KeySUYVUBYJARFZHO-RRKCRQDMSA-N
InChIInChI=1S/C10H16N5O12P3/c11-9-8-10(13-3-12-9)15(4-14-8)7-1-5(16)6(25-7)2-24-29(20,21)27-30(22,23)26-28(17,18)19/h3-7,16H,1-2H2,(H,20,21)(H,22,23)(H2,11,12,13)(H2,17,18,19)/t5-,6+,7+/m0/s1
IUPAC Name({[({[(2R,3S,5R)-5-(6-amino-9H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy](hydroxy)phosphoryl}oxy)phosphonic acid
Traditional IUPAC NamedATP
Chemical FormulaC10H16N5O12P3
SMILESNC1=NC=NC2=C1N=CN2[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1
Chemical Taxonomy
Description belongs to the class of organic compounds known as purine 2'-deoxyribonucleoside triphosphates. These are purine nucleotides with triphosphate group linked to the ribose moiety lacking a hydroxyl group at position 2.
KingdomOrganic compounds
Super ClassNucleosides, nucleotides, and analogues
ClassPurine nucleotides
Sub ClassPurine deoxyribonucleotides
Direct ParentPurine 2'-deoxyribonucleoside triphosphates
Alternative Parents
Substituents
  • Purine 2'-deoxyribonucleoside triphosphate
  • 6-aminopurine
  • Imidazopyrimidine
  • Purine
  • Aminopyrimidine
  • Monoalkyl phosphate
  • N-substituted imidazole
  • Organic phosphoric acid derivative
  • Phosphoric acid ester
  • Pyrimidine
  • Imidolactam
  • Alkyl phosphate
  • Azole
  • Imidazole
  • Heteroaromatic compound
  • Tetrahydrofuran
  • Secondary alcohol
  • Azacycle
  • Oxacycle
  • Organoheterocyclic compound
  • Organic oxygen compound
  • Primary amine
  • Organooxygen compound
  • Organonitrogen compound
  • Amine
  • Organic nitrogen compound
  • Organic oxide
  • Organopnictogen compound
  • Alcohol
  • Hydrocarbon derivative
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors
Physical Properties
StateSolid
Charge0
Melting pointNot Available
Experimental Properties
PropertyValueReference
Water SolubilityNot AvailablePhysProp
LogPNot AvailablePhysProp
Predicted Properties
PropertyValueSource
Water Solubility3.83 g/LALOGPS
logP-0.66ALOGPS
logP-4.9ChemAxon
logS-2.1ALOGPS
pKa (Strongest Acidic)0.9ChemAxon
pKa (Strongest Basic)4.03ChemAxon
Physiological Charge-3ChemAxon
Hydrogen Acceptor Count13ChemAxon
Hydrogen Donor Count6ChemAxon
Polar Surface Area258.9 ŲChemAxon
Rotatable Bond Count8ChemAxon
Refractivity94.3 m³·mol⁻¹ChemAxon
Polarizability38.06 ųChemAxon
Number of Rings3ChemAxon
Bioavailability0ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • cytoplasm
Organoleptic PropertiesNot Available
SMPDB Pathways
purine nucleotides de novo biosynthesisPW002478 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Purine metabolismec00230 Map00230
SMPDB Reactions
dADP + Adenosine triphosphateADP + dATP
Adenosine triphosphate + a reduced flavodoxin → an oxidized flavodoxin + water + dATP
KEGG Reactions
Guanosine monophosphate + dATPdADP + Guanosine diphosphate
Adenosine triphosphate + dADPdATP + ADP
Adenosine triphosphate + thioredoxin dithiol → dATP + thioredoxin disulfide + water
Concentrations
Intracellular Concentrations
Intracellular ConcentrationSubstrateGrowth ConditionsStrainCitation
44 ± 0 µM YEPD mediumaerobicBaker's yeastPMID: 14573610
Conversion Details Here
Extracellular ConcentrationsNot Available
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyView
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-002e-9843300000-a8d959008963a6e8a26cJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (1 TMS) - 70eV, Positivesplash10-007p-9218120000-4918f13056a529d12752JSpectraViewer
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-000f-0800900000-fa3d4e7a131ac1b4c8e7JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-000i-1900000000-91f17c669f5b4e231613JSpectraViewer | MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-000i-2900000000-66cc97431dd4c6ef5edbJSpectraViewer | MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-000i-0911200000-81436267b4eed8c39c3fJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-000i-0900000000-dad0a3294356131635d0JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-000i-1900000000-a1b841f4410b13c0280fJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-000i-0220900000-5fd893f07f0f264099fdJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-003r-5950100000-3901292643e421d47188JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-004i-9200000000-c3a099b6927fdfbe3098JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
2D NMR[1H,13C] 2D NMR SpectrumNot AvailableJSpectraViewer
References
References:
  • Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). "A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology." Nat Biotechnol 26:1155-1160.18846089
  • Chabes, A., Stillman, B. (2007). "Constitutively high dNTP concentration inhibits cell cycle progression and the DNA damage checkpoint in yeast Saccharomyces cerevisiae." Proc Natl Acad Sci U S A 104:1183-1188.17227840
  • Chabes, A., Georgieva, B., Domkin, V., Zhao, X., Rothstein, R., Thelander, L. (2003). "Survival of DNA damage in yeast directly depends on increased dNTP levels allowed by relaxed feedback inhibition of ribonucleotide reductase." Cell 112:391-401.12581528
  • Prieto, S., Bouillaud, F., Rial, E. (1996). "The nature and regulation of the ATP-induced anion permeability in Saccharomyces cerevisiae mitochondria." Arch Biochem Biophys 334:43-49.8837737
  • Coda-Zabetta, F., Boam, D. S. (1996). "Distinct effects of ATP on transcription complex formation and initiation in a yeast in vitro transcription system." Biochim Biophys Acta 1306:194-202.8634337
  • Muller, E. G. (1994). "Deoxyribonucleotides are maintained at normal levels in a yeast thioredoxin mutant defective in DNA synthesis." J Biol Chem 269:24466-24471.7929110
  • Koc, A., Wheeler, L. J., Mathews, C. K., Merrill, G. F. (2004). "Hydroxyurea arrests DNA replication by a mechanism that preserves basal dNTP pools." J Biol Chem 279:223-230.14573610
Synthesis Reference:Not Available
External Links:
ResourceLink
CHEBI ID16284
HMDB IDHMDB01532
Pubchem Compound ID15993
Kegg IDC00131
ChemSpider ID23105280
FOODB IDFDB022674
WikipediaDeoxyadenosine_triphosphate
BioCyc IDDATP

Enzymes

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. Required for repair of UV radiation- and etoposide-induced DNA damage
Gene Name:
YNK1
Uniprot ID:
P36010
Molecular weight:
17166.59961
Reactions
ATP + nucleoside diphosphate → ADP + nucleoside triphosphate.
General function:
Involved in protein binding
Specific function:
Essential for recycling GMP and indirectly, cGMP
Gene Name:
GUK1
Uniprot ID:
P15454
Molecular weight:
20637.19922
Reactions
ATP + GMP → ADP + GDP.
General function:
Involved in electron carrier activity
Specific function:
Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16, alkyl- hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2, alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex, it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER- derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism. Through its capacity to inactivate the stress response transcription factor YAP1 and its regulator the hydroperoxide stress sensor HYR1, it is involved in feedback regulation of stress response gene expression upon oxidative stress
Gene Name:
TRX2
Uniprot ID:
P22803
Molecular weight:
11203.7998
Reactions
General function:
Involved in electron carrier activity
Specific function:
Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16, alkyl- hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2, alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex, it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER- derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism
Gene Name:
TRX1
Uniprot ID:
P22217
Molecular weight:
11234.90039
Reactions