Record Information
Version2.0
Creation Date2012-05-31 09:55:42 -0600
Update Date2015-09-13 12:56:05 -0600
Secondary Accession Numbers
  • ECMDB00034
Identification
Name:Adenine
Description:Adenine is a purine base. Adenine is found in both DNA and RNA. Adenine is a fundamental component of adenine nucleotides. Adenine forms adenosine, a nucleoside, when attached to ribose, and deoxyadenosine when attached to deoxyribose; it forms adenosine triphosphate (ATP), a nucleotide, when three phosphate groups are added to adenosine. Adenosine triphosphate is used in cellular metabolism as one of the basic methods of transferring chemical energy between chemical reactions.
Structure
Thumb
Synonyms:
  • 1,6-Dihydro-6-iminopurine
  • 1H-Purin-6-amine
  • 1H-Purine-6-amine
  • 3,6-Dihydro-6-iminopurine
  • 6-Amino-1H-purine
  • 6-Amino-3H-purine
  • 6-Amino-7H-purine
  • 6-Amino-9H-purine
  • 6-Amino-Purine
  • 6-Aminopurine
  • 9H-Purin-6-amine
  • 9H-Purin-6-yl-amin
  • 9H-Purin-6-ylamine
  • 9H-Purine-6-amine
  • Ade
  • Adenin
  • Adenine
  • Adeninimine
  • Vitamin B4
Chemical Formula:C5H5N5
Weight:Average: 135.1267
Monoisotopic: 135.054495185
InChI Key:GFFGJBXGBJISGV-UHFFFAOYSA-N
InChI:InChI=1S/C5H5N5/c6-4-3-5(9-1-7-3)10-2-8-4/h1-2H,(H3,6,7,8,9,10)
CAS number:73-24-5
IUPAC Name:7H-purin-6-amine
Traditional IUPAC Name:vitamin B4
SMILES:NC1=C2NC=NC2=NC=N1
Chemical Taxonomy
DescriptionThis compound belongs to the class of organic compounds known as 6-aminopurines. These are purines that carry an amino group at position 6. Purine is a bicyclic aromatic compound made up of a pyrimidine ring fused to an imidazole ring.
KingdomOrganic compounds
Super ClassOrganoheterocyclic compounds
ClassImidazopyrimidines
Sub ClassPurines and purine derivatives
Direct Parent6-aminopurines
Alternative Parents
Substituents
  • 6-aminopurine
  • Aminopyrimidine
  • Imidolactam
  • Pyrimidine
  • Heteroaromatic compound
  • Imidazole
  • Azole
  • Azacycle
  • Organic nitrogen compound
  • Organopnictogen compound
  • Hydrocarbon derivative
  • Primary amine
  • Organonitrogen compound
  • Amine
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors
Physical Properties
State:Solid
Charge:0
Melting point:360 °C
Experimental Properties:
PropertyValueSource
Water Solubility:1.03 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)]PhysProp
LogP:-0.09 [HANSCH,C ET AL. (1995)]PhysProp
Predicted Properties
PropertyValueSource
Water Solubility11.5 mg/mLALOGPS
logP-0.38ALOGPS
logP-0.57ChemAxon
logS-1.1ALOGPS
pKa (Strongest Acidic)10.29ChemAxon
pKa (Strongest Basic)5.32ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count4ChemAxon
Hydrogen Donor Count2ChemAxon
Polar Surface Area80.48 Å2ChemAxon
Rotatable Bond Count0ChemAxon
Refractivity38.22 m3·mol-1ChemAxon
Polarizability12.29 Å3ChemAxon
Number of Rings2ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
Adenosine + Water > Adenine + Ribose
S-Adenosylhomocysteine + Water <> Adenine + S-Ribosyl-L-homocysteine
5'-Methylthioadenosine + Water > 5-Methylthioribose + Adenine
5'-Deoxyadenosine + Water > 5'-Deoxyribose + Adenine
Adenine + Phosphoribosyl pyrophosphate <> Adenosine monophosphate + Pyrophosphate
Adenosine triphosphate + Dephospho-CoA > 2'-(5-Triphosphoribosyl)-3'-dephospho-CoA + Adenine
Adenosine monophosphate + Water <> Adenine + D-Ribose-5-phosphate
Adenine + Hydrogen ion + Water > Hypoxanthine + Ammonium
Adenosine + Phosphate <> Adenine + Ribose-1-phosphate
Deoxyadenosine + Phosphate <> Deoxyribose 1-phosphate + Adenine
Adenosine monophosphate + Water <> Adenine + D-Ribose-5-phosphate
Adenosine monophosphate + Pyrophosphate <> Adenine + Phosphoribosyl pyrophosphate
S-Adenosylhomocysteine + Water <> S-Ribosyl-L-homocysteine + Adenine
Adenine + Water <> Hypoxanthine + Ammonia
Adenosine + Water <> Adenine + Ribose
5'-Methylthioadenosine + Water <> Adenine + 5-Methylthioribose
Adenosine + Phosphate <> Adenine + alpha-D-Ribose 1-phosphate
Deoxyadenosine + Phosphate <> Adenine + Deoxyribose 1-phosphate
5'-Deoxyadenosine + Water > 5'-Deoxyribose + Adenine
Methylphosphonate + Adenosine triphosphate > &alpha;-D-ribose-1-methylphosphonate-5-triphosphate + Adenine
Hydrogen ion + Dephospho-CoA + Adenosine triphosphate > 2'-(5-Triphosphoribosyl)-3'-dephospho-CoA + Adenine
Water + Adenine > Ammonia + Hypoxanthine
Adenosine + Water > D-ribose + Adenine
S-Ribosyl-L-homocysteine + Adenine < S-Adenosylhomocysteine + Water
Adenosine + Phosphate <> Ribose-1-phosphate + Adenine
Pyrophosphate + Adenosine monophosphate < Phosphoribosyl pyrophosphate + Adenine
Water + Adenosine monophosphate > D-Ribose-5-phosphate + Adenine
Deoxyadenosine + Phosphate <> Adenine + deoxyribose-1-phosphate
5'-Methylthioadenosine + Water > 5-Methylthioribose + Adenine
N1-Methyladenine + Oxygen + Oxoglutaric acid > Hydrogen ion + Adenine + Carbon dioxide + Formaldehyde + Succinic acid
1-Ethyladenine + Oxygen + Oxoglutaric acid > Adenine + Carbon dioxide + Acetaldehyde + Succinic acid
Adenine + Water > Hypoxanthine + Ammonia
Adenosine monophosphate + Water > D-Ribose-5-phosphate + Adenine
Adenosine monophosphate + Pyrophosphate > Adenine + Phosphoribosyl pyrophosphate
Adenosine triphosphate + Dephospho-CoA > 2'-(5-Triphosphoribosyl)-3'-dephospho-CoA + Adenine
S-Adenosylhomocysteine + Water > S-Ribosyl-L-homocysteine + Adenine
5'-Methylthioadenosine + Water > S-methyl-5-thio-D-ribose + Adenine
S-adenosyl-L-methionine + 7-Aminomethyl-7-deazaguanosine > L-Methionine + Adenine + epoxyqueuosine
Adenosine triphosphate + Dephospho-CoA <> 2'-(5-Triphosphoribosyl)-3'-dephospho-CoA + Adenine
Adenosine triphosphate + Methylphosphonate <> alpha-D-Ribose 1-methylphosphonate 5-triphosphate + Adenine
S-Adenosylhomocysteine + Water > Adenine + S-ribosyl-L-homocysteine + S-ribosyl-L-homocysteine
5'-S-methyl-5'-thioadenosine + Water > 5-Methylthioribose + Adenine
7-aminomethyl-7-deazaguanosine34 in tRNA + S-adenosyl-L-methionine > Hydrogen ion + L-Methionine + Adenine + epoxyqueuosine
1-Ethyladenine + Oxoglutaric acid + Oxygen > Adenine + Carbon dioxide + Acetaldehyde + Succinic acid
S-Adenosylhomocysteine + Water > Adenine
Adenosine + Water > beta-D-ribofuranose + Adenine
Methylphosphonate + Adenosine triphosphate > Adenine + alpha-D-Ribose 1-methylphosphonate 5-triphosphate
Adenine + Ribose-1-phosphate > Phosphate + Adenosine
Adenosine + Phosphate > Adenine + Ribose-1-phosphate
Deoxyadenosine + Phosphate > Adenine + Deoxyribose 1-phosphate
Adenine + Phosphoribosyl pyrophosphate > Pyrophosphate + Adenosine monophosphate
Dephospho-CoA + Adenosine triphosphate + Hydrogen ion > Adenine + 2'-(5-Triphosphoribosyl)-3'-dephospho-CoA
Adenosine monophosphate + Water > D-Ribose-5-phosphate + Adenine
More...

SMPDB Pathways:
Citrate lyase activationPW002075 Pw002075Pw002075 greyscalePw002075 simple
Collection of Reactions without pathwaysPW001891 Pw001891Pw001891 greyscalePw001891 simple
Pantothenate and CoA biosynthesisPW000828 Pw000828Pw000828 greyscalePw000828 simple
Quorum SensingPW000836 Pw000836Pw000836 greyscalePw000836 simple
S-adenosyl-L-methionine biosynthesisPW000837 Pw000837Pw000837 greyscalePw000837 simple
S-adenosyl-L-methionine cyclePW002080 Pw002080Pw002080 greyscalePw002080 simple
Spermidine biosynthesis and metabolismPW002085 Pw002085Pw002085 greyscalePw002085 simple
adenine and adenosine salvage IPW002069 Pw002069Pw002069 greyscalePw002069 simple
adenine and adenosine salvage IIPW002071 Pw002071Pw002071 greyscalePw002071 simple
adenine and adenosine salvage IIIPW002072 Pw002072Pw002072 greyscalePw002072 simple
methylphosphonate degradation IPW002065 Pw002065Pw002065 greyscalePw002065 simple
preQ0 metabolismPW001893 Pw001893Pw001893 greyscalePw001893 simple
purine deoxyribonucleosides degradationPW002077 Pw002077Pw002077 greyscalePw002077 simple
purine ribonucleosides degradationPW002076 Pw002076Pw002076 greyscalePw002076 simple
KEGG Pathways:
EcoCyc Pathways:
  • 2'-(5'-phosphoribosyl)-3'-dephospho-CoA biosynthesis I (citrate lyase) P2-PWY
  • S-adenosyl-L-methionine cycle I PWY-6151
  • S-methyl-5'-thioadenosine degradation IV PWY0-1391
  • adenine and adenosine salvage II PWY-6605
  • adenine and adenosine salvage III PWY-6609
  • adenine and adenosine salvage V PWY-6611
  • adenosine nucleotides degradation III PWY-6617
  • autoinducer AI-2 biosynthesis I PWY-6153
  • methylphosphonate degradation PWY0-1533
  • purine deoxyribonucleosides degradation PWY0-1297
  • purine ribonucleosides degradation to ribose-1-phosphate PWY0-1296
  • queuosine biosynthesis PWY-6700
Concentrations
ConcentrationStrainMediaGrowth StatusGrowth SystemTemperatureDetails
1± 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
1± 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
1± 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
102± 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
34± 10 uMBL21 DE3Luria-Bertani (LB) mediaStationary phase cultures (overnight culture)Shake flask37 oCExperimentally Determined
Download Details
Find out more about how we convert literature concentrations.
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (2 TMS)splash10-03di-3490000000-7efe9518c90307a43707View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies)splash10-03di-2690000000-6dc072eb8483a2c38e18View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (2 TMS)splash10-00di-9350000000-220125189c286547e86cView in MoNA
GC-MSGC-MS Spectrum - GC-MS (2 TMS)splash10-03di-4690000000-2d327a6944df53411886View in MoNA
GC-MSGC-MS Spectrum - GC-MS (1 TMS)splash10-0006-3920000000-f488e8aa64272a07b3d9View in MoNA
GC-MSGC-MS Spectrum - GC-MS (3 TMS)splash10-000i-0329000000-0b012fa483ce8764d2afView in MoNA
GC-MSGC-MS Spectrum - GC-MSNot Available
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-000i-0900000000-95d4894082ada0b24773View in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-014i-5900000000-66b1c086d7a666b2d02bView in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-014i-9200000000-4202a1aec437f3fd1275View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-000i-0900000000-c1766360e5f779d277abView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-000i-0900000000-68585e8dac03a15d5210View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-014i-0900000000-3db475b164c0f884b93dView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-014i-2900000000-7e2deed118def434e8dbView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0a4i-0900000000-b24b09629456779d96e6View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF (UPLC Q-Tof Premier, Waters) , Positivesplash10-000i-0900000000-b2cc6b5ce2fe2affe47dView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF (UPLC Q-Tof Premier, Waters) 30V, Positivesplash10-000i-0900000000-f45a65a00be3c0c36350View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF (UPLC Q-Tof Premier, Waters) , Negativesplash10-001i-0900000000-80808f34c7497219d349View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF (UPLC Q-Tof Premier, Waters) 30V, Negativesplash10-0a5c-6900000000-f6c0abd6d3fca61bd7f7View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-000i-0900000000-f2335984e7dd7e129a8cView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-000i-0900000000-ee084d257bf2325fb370View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-067i-9700000000-5a42850e3f5331952458View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-001i-0900000000-05fa9674ab4d9e5e174eView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-001i-0900000000-dc404aa4196bbf0ae9cdView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-05o0-8900000000-b56d110371cd80ac76e0View in MoNA
MSMass Spectrum (Electron Ionization)splash10-000i-6900000000-39944576233751576a91View in MoNA
1D NMR1H NMR SpectrumNot Available
1D NMR1H NMR SpectrumNot Available
1D NMR13C NMR SpectrumNot Available
2D NMR[1H,1H] 2D 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
  • Di Pietro V, Perruzza I, Amorini AM, Balducci A, Ceccarelli L, Lazzarino G, Barsotti P, Giardina B, Tavazzi B: Clinical, biochemical and molecular diagnosis of a compound homozygote for the 254 bp deletion-8 bp insertion of the APRT gene suffering from severe renal failure. Clin Biochem. 2006 Oct 19;. Pubmed: 17126311
  • Eells JT, Spector R: Purine and pyrimidine base and nucleoside concentrations in human cerebrospinal fluid and plasma. Neurochem Res. 1983 Nov;8(11):1451-7. Pubmed: 6656991
  • Hartmann S, Okun JG, Schmidt C, Langhans CD, Garbade SF, Burgard P, Haas D, Sass JO, Nyhan WL, Hoffmann GF: Comprehensive detection of disorders of purine and pyrimidine metabolism by HPLC with electrospray ionization tandem mass spectrometry. Clin Chem. 2006 Jun;52(6):1127-37. Epub 2006 Apr 13. Pubmed: 16613999
  • 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
  • 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
  • Liu Y, Xu G, Xu C, Garcia L, Lin CC, Yeh LT: Ultra sensitive method for the determination of 9-(2-phosphonylmethoxyethyl)adenine in human serum by liquid chromatography-tandem mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2004 Apr 25;803(2):293-8. Pubmed: 15063338
  • Moriyama H, Iizuka T, Nagai M, Hoshi K: Adenine, an inhibitor of platelet aggregation, from the leaves of Cassia alata. Biol Pharm Bull. 2003 Sep;26(9):1361-4. Pubmed: 12951489
  • Ohdoi C, Nyhan WL, Kuhara T: Chemical diagnosis of Lesch-Nyhan syndrome using gas chromatography-mass spectrometry detection. J Chromatogr B Analyt Technol Biomed Life Sci. 2003 Jul 15;792(1):123-30. Pubmed: 12829005
  • Reimers HJ, Packham MA, Mustard JF: Labeling of the releasable adenine nucleotides of washed human platelets. Blood. 1977 Jan;49(1):89-99. Pubmed: 401462
  • Rolfes RJ: Regulation of purine nucleotide biosynthesis: in yeast and beyond. Biochem Soc Trans. 2006 Nov;34(Pt 5):786-90. Pubmed: 17052198
  • Ruiz-Stewart I, Kazerounian S, Pitari GM, Schulz S, Waldman SA: Soluble guanylate cyclase is allosterically inhibited by direct interaction with 2-substituted adenine nucleotides. Eur J Biochem. 2002 Apr;269(8):2186-93. Pubmed: 11985597
  • Simoni RE, Gomes LN, Scalco FB, Oliveira CP, Aquino Neto FR, de Oliveira ML: Uric acid changes in urine and plasma: an effective tool in screening for purine inborn errors of metabolism and other pathological conditions. J Inherit Metab Dis. 2007 Jun;30(3):295-309. Epub 2007 May 19. Pubmed: 17520339
  • Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4. Pubmed: 19212411
  • Steiner MC, Evans R, Deacon SJ, Singh SJ, Patel P, Fox J, Greenhaff PL, Morgan MD: Adenine nucleotide loss in the skeletal muscles during exercise in chronic obstructive pulmonary disease. Thorax. 2005 Nov;60(11):932-6. Epub 2005 Jul 29. Pubmed: 16055624
  • Terry KL, De Vivo I, Titus-Ernstoff L, Shih MC, Cramer DW: Androgen receptor cytosine, adenine, guanine repeats, and haplotypes in relation to ovarian cancer risk. Cancer Res. 2005 Jul 1;65(13):5974-81. Pubmed: 15994977
  • 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
  • Vijayendran, C., Barsch, A., Friehs, K., Niehaus, K., Becker, A., Flaschel, E. (2008). "Perceiving molecular evolution processes in Escherichia coli by comprehensive metabolite and gene expression profiling." Genome Biol 9:R72. Pubmed: 18402659
  • Whitehead JW, Lee GP, Gharagozloo P, Hofer P, Gehrig A, Wintergerst P, Smyth D, McCoull W, Hachicha M, Patel A, Kyle DJ: 8-Substituted analogues of 3-(3-cyclopentyloxy-4-methoxy-benzyl)-8-isopropyl-adenine: highly potent and selective PDE4 inhibitors. J Med Chem. 2005 Feb 24;48(4):1237-43. Pubmed: 15715490
  • Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948. Pubmed: 18331064
Synthesis Reference:Baddiley, J.; Lythgoe, B.; Todd, A. R. Synthesis of purine nucleosides. II. A new and convenient synthesis of adenine. Journal of the Chemical Society (1943), 386-7.
Material Safety Data Sheet (MSDS)Download (PDF)
External Links:
ResourceLink
CHEBI ID16708
HMDB IDHMDB00034
Pubchem Compound ID190
Kegg IDC00147
ChemSpider ID185
WikipediaAdenine
BioCyc IDADENINE
EcoCyc IDADENINE
Ligand ExpoANE

Enzymes

General function:
Involved in hypoxanthine phosphoribosyltransferase activity
Specific function:
This enzyme acts exclusively on hypoxanthine; it does not act on guanine
Gene Name:
hpt
Uniprot ID:
P0A9M2
Molecular weight:
20115
Reactions
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate.
General function:
Involved in purine-nucleoside phosphorylase activity
Specific function:
Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules
Gene Name:
deoD
Uniprot ID:
P0ABP8
Molecular weight:
25950
Reactions
Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate.
General function:
Involved in catalytic activity
Specific function:
Involved in regulation of AMP concentrations
Gene Name:
amn
Uniprot ID:
P0AE12
Molecular weight:
53994
Reactions
AMP + H(2)O = D-ribose 5-phosphate + adenine.
General function:
Involved in adenosylhomocysteine nucleosidase activity
Specific function:
Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S- adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Can also use 5'-isobutylthioadenosine, 5'-n- butylthioadenosine, S-adenosyl-D-homocysteine, decarboxylated adenosylhomocysteine, deaminated adenosylhomocysteine and S-2-aza- adenosylhomocysteine as substrates
Gene Name:
mtnN
Uniprot ID:
P0AF12
Molecular weight:
24354
Reactions
S-adenosyl-L-homocysteine + H(2)O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine.
S-methyl-5'-thioadenosine + H(2)O = S-methyl-5-thio-D-ribose + adenine.
General function:
Involved in riboflavin synthase activity
Specific function:
Riboflavin synthase is a bifunctional enzyme complex catalyzing the formation of riboflavin from 5-amino-6-(1'-D)- ribityl-amino-2,4(1H,3H)-pyrimidinedione and L-3,4-dihydrohy-2- butanone-4-phosphate via 6,7-dimethyl-8-lumazine. The alpha subunit catalyzes the dismutation of 6,7-dimethyl-8-lumazine to riboflavin and 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)- pyrimidinedione
Gene Name:
ribE
Uniprot ID:
P0AFU8
Molecular weight:
23445
Reactions
2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine.
General function:
Involved in hydrolase activity, hydrolyzing N-glycosyl compounds
Specific function:
Hydrolyzes both purine and pyrimidine ribonucleosides with a broad-substrate specificity with decreasing activity in the order uridine, xanthosine, inosine, adenosine, cytidine, guanosine
Gene Name:
rihC
Uniprot ID:
P22564
Molecular weight:
32560
General function:
Involved in adenine deaminase activity
Specific function:
Adenine + H(2)O = hypoxanthine + NH(3)
Gene Name:
ade
Uniprot ID:
P31441
Molecular weight:
63739
Reactions
Adenine + H(2)O = hypoxanthine + NH(3).
General function:
Involved in hydrolase activity, hydrolyzing N-glycosyl compounds
Specific function:
Hydrolyzes cytidine or uridine to ribose and cytosine or uracil, respectively. Has a clear preference for cytidine over uridine. Strictly specific for ribonucleosides. Has a low but significant activity for the purine nucleoside xanthosine
Gene Name:
rihB
Uniprot ID:
P33022
Molecular weight:
33748
Reactions
A pyrimidine nucleoside + H(2)O = D-ribose + a pyrimidine base.
General function:
Involved in adenine phosphoribosyltransferase activity
Specific function:
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis
Gene Name:
apt
Uniprot ID:
P69503
Molecular weight:
19859
Reactions
AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate.
General function:
Involved in ATP binding
Specific function:
Catalyzes the formation of 2-(5''-triphosphoribosyl)-3'- dephosphocoenzyme-A, the precursor of the prosthetic group of the holo-acyl carrier protein (gamma chain) of citrate lyase, from ATP and dephospho-CoA
Gene Name:
citG
Uniprot ID:
P77231
Molecular weight:
31644
Reactions
ATP + 3-dephospho-CoA = 2'-(5-triphosphoribosyl)-3'-dephospho-CoA + adenine.
General function:
Not Available
Specific function:
Dioxygenase that repairs alkylated DNA and RNA containing 3-methylcytosine or 1-methyladenine by oxidative demethylation. Has highest activity towards 3-methylcytosine. Has lower activity towards alkylated DNA containing ethenoadenine, and no detectable activity towards 1-methylguanine or 3-methylthymine. Accepts double-stranded and single-stranded substrates. Requires molecular oxygen, alpha-ketoglutarate and iron. Provides extensive resistance to alkylating agents such as MMS and DMS (SN2 agents), but not to MMNG and MNU (SN1 agents). Dioxygenase that repairs alkylated DNA and RNA containing 3-methylcytosine or 1-methyladenine by oxidative demethylation. Has highest activity towards 3-methylcytosine. Has lower activity towards alkylated DNA containing ethenoadenine, and no detectable activity towards 1-methylguanine or 3-methylthymine. Accepts double-stranded and single-stranded substrates. Requires molecular oxygen, alpha-ketoglutarate and iron. Provides extensive resistance to alkylating agents such as MMS and DMS (SN2 agents), but not to MMNG and MNU (SN1 agents).
Gene Name:
alkB
Uniprot ID:
P05050
Molecular weight:
Not Available
Reactions
DNA-base-CH(3) + 2-oxoglutarate + O(2) = DNA-base + formaldehyde + succinate + CO(2).
DNA-base-CH(3) + 2-oxoglutarate + O(2) = DNA-base + formaldehyde + succinate + CO(2).
General function:
Translation, ribosomal structure and biogenesis
Specific function:
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA)
Gene Name:
queA
Uniprot ID:
P0A7F9
Molecular weight:
39430
Reactions
S-adenosylmethionine + 7-aminomethyl-7-deazaguanosine = methionine + adenine + epoxyqueuosine.
General function:
organic phosphonate catabolic process
Specific function:
Together with PhnG, PhnH and PhnI is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate.
Gene Name:
phnL
Uniprot ID:
P16679
Molecular weight:
24705
Reactions
ATP + methylphosphonate = alpha-D-ribose 1-methylphosphonate 5-triphosphate + adenine
General function:
organic phosphonate catabolic process
Specific function:
Together with PhnG, PhnH and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate. PhnI alone has nucleosidase activity, catalyzing the hydrolysis of ATP or GTP forming alpha-D-ribose 5-triphosphate and adenine or guanine, respectively.
Gene Name:
phnI
Uniprot ID:
P16687
Molecular weight:
38852
Reactions
ATP + methylphosphonate = alpha-D-ribose 1-methylphosphonate 5-triphosphate + adenine
General function:
organic phosphonate catabolic process
Specific function:
Together with PhnG, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate.
Gene Name:
phnH
Uniprot ID:
P16686
Molecular weight:
21027
Reactions
ATP + methylphosphonate = alpha-D-ribose 1-methylphosphonate 5-triphosphate + adenine
General function:
organic phosphonate transport
Specific function:
Together with PhnH, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate.
Gene Name:
phnG
Uniprot ID:
P16685
Molecular weight:
16539
Reactions
ATP + methylphosphonate = alpha-D-ribose 1-methylphosphonate 5-triphosphate + adenine

Transporters

General function:
Involved in transporter activity
Specific function:
Specific, proton motive force-dependent high-affinity transporter for xanthine
Gene Name:
xanP
Uniprot ID:
P0AGM9
Molecular weight:
48868
General function:
Involved in transporter activity
Specific function:
High-affinity uptake of adenine
Gene Name:
purP
Uniprot ID:
P31466
Molecular weight:
46865
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
General function:
organic phosphonate transport
Specific function:
Together with PhnH, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate.
Gene Name:
phnG
Uniprot ID:
P16685
Molecular weight:
16539
Reactions
ATP + methylphosphonate = alpha-D-ribose 1-methylphosphonate 5-triphosphate + adenine