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targets (12) enzymes (1)
for drugs
Identification
Name Adenine
Accession Number DB00173 (EXPT00520, NUTR00012)
Type small molecule
Groups approved, nutraceutical
Description

A purine base and a fundamental unit of adenine nucleotides. [PubChem]
Structure Thumb
Download: MOL | SDF | SMILES | InChI
Display: 2D Structure | 3D Structure
Synonyms
1H-Purin-6-amine
6-Aminopurine
Adenin
Adeninimine
Vitamin B4
Salts Not Available
Brand names
Name Company
Leuco-4
Pedatisectine B
Brand mixtures Not Available
Categories
  • Dietary supplement
  • Micronutrient
CAS number 73-24-5
Weight Average: 135.1267
Monoisotopic: 135.054495185
Chemical Formula C5H5N5
InChI Key InChIKey=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)
Plain Text
IUPAC Name
7H-purin-6-amine
SMILES
NC1=C2NC=NC2=NC=N1
Plain Text
Mass Spec show (7.29 KB)
Taxonomy
Kingdom Organic
Classes
  • Purines and Purine Derivatives
Substructures
  • Aliphatic and Aryl Amines
  • Pyrimidines and Derivatives
  • Imidazoles
  • Heterocyclic compounds
  • Aromatic compounds
  • Purines and Purine Derivatives
  • Cyanamides
Pharmacology
Indication For nutritional supplementation, also for treating dietary shortage or imbalance
Pharmacodynamics Adenine (sometimes known as vitamin B4) combines with the sugar ribose to form adenosine, which in turn can be bonded with from one to three phosphoric acid units, yielding AMP, ADP and ATP . These adenine derivatives perform important functions in cellular metabolism. Adenine is one of four nitrogenous bases utilized in the synthesis of nucleic acids. A modified form of adenosine monophosphate (cyclic AMP) is an imporant secondary messenger in the propagation of many hormonal stimuli. Adenine is an integral part of the structure of many coenzymes. Adenosine (adenine with a ribose group) causes transient heart block in the AV node of the heart. In individuals suspected of suffering from a supraventricular tachycardia (SVT), adenosine is used to help identify the rhythm. Certain SVTs can be successfully terminated with adenosine.
Mechanism of action Adenine forms adenosine, a nucleoside, when attached to ribose, and deoxyadenosine when attached to deoxyribose, and 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 reactions. In older literature, adenine was sometimes called Vitamin B4Not Available
Absorption Not Available
Volume of distribution Not Available
Protein binding Not Available
Metabolism Not Available
Route of elimination Not Available
Half life Not Available
Clearance Not Available
Toxicity Not Available
Affected organisms
  • Humans and other mammals
Pathways Not Available
Pharmacoeconomics
Manufacturers Not Available
Packagers Not Available
Dosage forms Not Available
Prices Not Available
Patents Not Available
Properties
State solid
Experimental Properties
Property Value Source
melting point 360 dec °C PhysProp
water solubility 1030 mg/L (at 25 °C) YALKOWSKY,SH & DANNENFELSER,RM (1992)
logP -0.09 HANSCH,C ET AL. (1995)
logS -2.12 ADME Research, USCD
pKa 4.15 (at 25 °C) KORTUM,G ET AL (1961)
Predicted Properties
Property Value Source
water solubility 1.15e+01 g/l ALOGPS
logP -0.38 ALOGPS
logP -0.57 ChemAxon
logS -1.1 ALOGPS
pKa (strongest acidic) 10.29 ChemAxon
pKa (strongest basic) 5.32 ChemAxon
physiological charge 0 ChemAxon
hydrogen acceptor count 4 ChemAxon
hydrogen donor count 2 ChemAxon
polar surface area 80.48 ChemAxon
rotatable bond count 0 ChemAxon
refractivity 38.22 ChemAxon
polarizability 12.29 ChemAxon
References
Synthesis Reference Not Available
General Reference Not Available
External Links
Resource Link
KEGG Drug D00034 Link_out
KEGG Compound C00147 Link_out
PubChem Compound 190 Link_out
PubChem Substance 46507319 Link_out
ChemSpider 185 Link_out
BindingDB 33218 Link_out
ChEBI 16708 Link_out
ChEMBL 16708 Link_out
Therapeutic Targets Database DAP000982 Link_out
PharmGKB PA448048 Link_out
HET ADE Link_out
Wikipedia http://en.wikipedia.org/wiki/Adenine Link_out
ATC Codes Not Available
AHFS Codes Not Available
PDB Entries
FDA label Not Available
MSDS show (72.5 KB)
Interactions
Drug Interactions Not Available
Food Interactions Not Available
Targets

1. Adenine phosphoribosyltransferase

Pharmacological action: unknown

Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis

Organism class: human
UniProt ID: P07741 Link_out
Gene: APRT Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Barrett C, Alley J, Pulido JC, Spurling H, Li P, Parsons T, Mallender WD, Bembenek ME: Configuration of a scintillation proximity assay for the activity assessment of recombinant human adenine phosphoribosyltransferase. Assay Drug Dev Technol. 2006 Dec;4(6):661-9. Pubmed
  2. 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. 2007 Jan;40(1-2):73-80. Epub 2006 Oct 19. Pubmed
  3. Katahira R, Ashihara H: Profiles of purine biosynthesis, salvage and degradation in disks of potato (Solanum tuberosum L.) tubers. Planta. 2006 Dec;225(1):115-26. Epub 2006 Jul 15. Pubmed
  4. Katahira R, Ashihara H: Role of adenosine salvage in wound-induced adenylate biosynthesis in potato tuber slices. Plant Physiol Biochem. 2006 Oct;44(10):551-5. Epub 2006 Oct 9. Pubmed
  5. Boitz JM, Ullman B: Leishmania donovani singly deficient in HGPRT, APRT or XPRT are viable in vitro and within mammalian macrophages. Mol Biochem Parasitol. 2006 Jul;148(1):24-30. Epub 2006 Mar 15. Pubmed
  6. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed

2. MTA/SAH nucleosidase

Pharmacological action: unknown

Responsible for cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH)

Organism class: bacterial
UniProt ID: P0AF12 Link_out
Gene: mtnN
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed
  3. Singh V, Lee JE, Nunez S, Howell PL, Schramm VL: Transition state structure of 5’-methylthioadenosine/S-adenosylhomocysteine nucleosidase from Escherichia coli and its similarity to transition state analogues. Biochemistry. 2005 Sep 6;44(35):11647-59. Pubmed
  4. Walker RD, Duerre JA: S-adenosylhomocysteine metabolism in various species. Can J Biochem. 1975 Mar;53(3):312-9. Pubmed
  5. Singh V, Schramm VL: Transition-state analysis of S. pneumoniae 5’-methylthioadenosine nucleosidase. J Am Chem Soc. 2007 Mar 14;129(10):2783-95. Epub 2007 Feb 14. Pubmed

3. Acetyl-CoA carboxylase 2

Pharmacological action: unknown

ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. This protein carries three functions:biotin carboxyl carrier protein, biotin carboxylase, and carboxyltransferase

Organism class: human
UniProt ID: O00763 Link_out
Gene: ACACB Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed
  3. Rasmussen JT, Rosendal J, Knudsen J: Interaction of acyl-CoA binding protein (ACBP) on processes for which acyl-CoA is a substrate, product or inhibitor. Biochem J. 1993 Jun 15;292 ( Pt 3):907-13. Pubmed
  4. Witters LA, Mendel DB, Colliton JW: Modulation of acetyl-CoA carboxylase by inhibitors of IMP dehydrogenase: implications for insulin regulation. Arch Biochem Biophys. 1987 Jan;252(1):130-5. Pubmed
  5. Itani SI, Saha AK, Kurowski TG, Coffin HR, Tornheim K, Ruderman NB: Glucose autoregulates its uptake in skeletal muscle: involvement of AMP-activated protein kinase. Diabetes. 2003 Jul;52(7):1635-40. Pubmed
  6. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed

4. Low molecular weight phosphotyrosine protein phosphatase

Pharmacological action: unknown

Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Isoform 3 does not possess phosphatase activity

Organism class: human
UniProt ID: P24666 Link_out
Gene: ACP1 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed
  3. Wang S, Stauffacher CV, Van Etten RL: Structural and mechanistic basis for the activation of a low-molecular weight protein tyrosine phosphatase by adenine. Biochemistry. 2000 Feb 15;39(6):1234-42. Pubmed
  4. Magherini F, Gamberi T, Paoli P, Marchetta M, Biagini M, Raugei G, Camici G, Ramponi G, Modesti A: The in vivo tyrosine phosphorylation level of yeast immunophilin Fpr3 is influenced by the LMW-PTP Ltp1. Biochem Biophys Res Commun. 2004 Aug 20;321(2):424-31. Pubmed
  5. Ostanin K, Pokalsky C, Wang S, Van Etten RL: Cloning and characterization of a Saccharomyces cerevisiae gene encoding the low molecular weight protein-tyrosine phosphatase. J Biol Chem. 1995 Aug 4;270(31):18491-9. Pubmed
  6. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed

5. Peroxisomal trans-2-enoyl-CoA reductase

Pharmacological action: unknown

Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity

Organism class: human
UniProt ID: Q9BY49 Link_out
Gene: PECR
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

6. A/G-specific adenine glycosylase

Pharmacological action: unknown

Adenine glycosylase active on G-A mispairs. MutY also corrects error-prone DNA synthesis past go lesions which are due to the oxidatively damaged form of guanine:7,8-dihydro-8- oxoguanine

Organism class: bacterial
UniProt ID: P17802 Link_out
Gene: mutY
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

7. Purine trans deoxyribosylase

Pharmacological action: unknown
Organism class: bacterial
UniProt ID: Q8RLY5 Link_out
Gene: ptd
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

8. Serine/threonine-protein kinase SRPK2

Pharmacological action: unknown

Phosphorylates RS domain-containing proteins, such as SFRS1 and SFRS2 on serine residues. Role in spliceosome assembly and in mediating the trafficking of splicing factors. Appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids

Organism class: human
UniProt ID: P78362 Link_out
Gene: SRPK2 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. Pubmed

9. Holliday junction ATP-dependent DNA helicase ruvB

Pharmacological action: unknown

The ruvA-ruvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is an helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvB is a Mg(2+)-dependent, DNA-dependent ATPase with an equal preference for supercoiled and linear duplex DNA. It can promote Holliday junction migration alone

Organism class: bacterial
UniProt ID: Q5SL87 Link_out
Gene: ruvB
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

10. DNA

Pharmacological action: unknown

DNA is the molecule of heredity, as it is responsible for the genetic propagation of most inherited traits. It is a polynucleic acid that carries genetic information on cell growth, division, and function. DNA consists of two long strands of nucleotides twisted into a double helix and held together by hydrogen bonds. The sequence of nucleotides determines hereditary characteristics. Each strand serves as the template for subsequent DNA replication and as a template for mRNA production, leading to protein synthesis via ribosomes.

Gene Sequence: FASTA

References:
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed
  3. Simon R, Heithoff DM, Mahan MJ, Samuel CE: Tissue Selective Proinflammatory Gene Induction in Mice Infected with Wild-Type Compared to DNA Adenine Methylase- or Flagella-deficient Salmonella. Infect Immun. 2007 Sep 24;. Pubmed
  4. Ichida H, Maeda K, Ichise H, Matsuyama T, Abe T, Yoneyama K, Koba T: In silico restriction landmark genome scanning analysis of Xanthomonas oryzae pathovar oryzae MAFF 311018. Biochem Biophys Res Commun. 2007 Nov 23;363(3):852-6. Epub 2007 Sep 24. Pubmed
  5. Mamdouh W, Dong M, Kelly RE, Kantorovich LN, Besenbacher F: Coexistence of Homochiral and Heterochiral Adenine Domains at the Liquid/Solid Interface. J Phys Chem B. 2007 Oct 5;. Pubmed

11. S-methyl-5-thioadenosine phosphorylase

Pharmacological action: unknown

Plays a major role in polyamine metabolism and is important for the salvage of both adenine and methionine

Organism class: human
UniProt ID: Q13126 Link_out
Gene: MTAP Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Chow WA, Bedell V, Gaytan P, Borden E, Goldblum J, Hicks D, Slovak ML: Methylthioadenosine phosphorylase gene deletions are frequently detected by fluorescence in situ hybridization in conventional chondrosarcomas. Cancer Genet Cytogenet. 2006 Apr 15;166(2):95-100. Pubmed
  2. Chattopadhyay S, Zhao R, Tsai E, Schramm VL, Goldman ID: The effect of a novel transition state inhibitor of methylthioadenosine phosphorylase on pemetrexed activity. Mol Cancer Ther. 2006 Oct;5(10):2549-55. Pubmed
  3. Singh V, Schramm VL: Transition-state structure of human 5’-methylthioadenosine phosphorylase. J Am Chem Soc. 2006 Nov 15;128(45):14691-6. Pubmed

12. Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase

Pharmacological action: unknown

Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6- dimethylbenzimidazole (DMB)

Organism class: bacterial
UniProt ID: Q05603 Link_out
Gene: cobT
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed
  3. Maggio-Hall LA, Escalante-Semerena JC: Alpha-5,6-dimethylbenzimidazole adenine dinucleotide (alpha-DAD), a putative new intermediate of coenzyme B12 biosynthesis in Salmonella typhimurium. Microbiology. 2003 Apr;149(Pt 4):983-90. Pubmed
  4. Cheong CG, Escalante-Semerena JC, Rayment I: Structural investigation of the biosynthesis of alternative lower ligands for cobamides by nicotinate mononucleotide: 5,6-dimethylbenzimidazole phosphoribosyltransferase from Salmonella enterica. J Biol Chem. 2001 Oct 5;276(40):37612-20. Epub 2001 Jul 5. Pubmed
  5. Trzebiatowski JR, Escalante-Semerena JC: Purification and characterization of CobT, the nicotinate-mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase enzyme from Salmonella typhimurium LT2. J Biol Chem. 1997 Jul 11;272(28):17662-7. Pubmed
Enzymes

1. UDP-glucuronosyltransferase 1-1

Actions: inhibitor

UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform glucuronidates bilirubin IX- alpha to form both the IX-alpha-C8 and IX-alpha-C12 monoconjugates and diconjugate

UniProt ID: P22309 Link_out
Gene: UGT1A1 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
SNPs: SNPJam Report Link_out

References:
  1. Nishimura Y, Maeda S, Ikushiro S, Mackenzie PI, Ishii Y, Yamada H: Inhibitory effects of adenine nucleotides and related substances on UDP-glucuronosyltransferase: structure-effect relationships and evidence for an allosteric mechanism. Biochim Biophys Acta. 2007 Nov;1770(11):1557-66. Epub 2007 Aug 8. Pubmed
Comments
Drug created on June 13, 2005 07:24 / Updated on February 08, 2013 16:19