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MetaCyc Pathway: adenine and adenosine salvage I
Inferred from experiment

Enzyme View:

Pathway diagram: adenine and adenosine salvage I

This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Synonyms: purine salvage, salvage pathway of adenosine nucleosides, adenosine nucleosides salvage I

Superclasses: BiosynthesisNucleosides and Nucleotides BiosynthesisPurine Nucleotide BiosynthesisPurine Nucleotide SalvageAdenine and Adenosine Salvage

Some taxa known to possess this pathway include : Halobacterium salinarum, Homo sapiens, Mycoplasma pneumoniae M129

Expected Taxonomic Range: Archaea, Bacteria , Opisthokonta

Adenosine nucleotides can be synthesized de novo. In that route AMP (AMP) is synthesized via IMP (IMP) and adenylo-succinate , which is converted to AMP by the action of adenylosuccinate lyase (see superpathway of adenosine nucleotides de novo biosynthesis II). Note that the free base adenine or the ribonucleoside adenosine are not produced via the de novo pathway.

Many organisms can also recycle adenosine nucleotides by a combination of degradation and salvage pathways. The degradation pathways are responsible for the conversion of the nucleotides to the nucleoside ( adenosine) and free base form ( adenine), and further degradation to compounds that can be catabolized to basic building blocks (for example, see adenosine nucleotides degradation II).

However, both adenosine and adenine can be salvaged by certain enzymes, and be converted back to nucleotide form.

The enzyme purine phosphorylase (DeoD) (EC cleaves adenosine to adenine and α-D-ribose-1-phosphate, while a second enzyme, such as adenine phosphoribosyltransferase, can utilize 5-phospho-α-D-ribose 1-diphosphate to convert the free base to the mononucleotide AMP.

Other routes from adenosine to AMP are described in adenine and adenosine salvage II and adenine and adenosine salvage VI.

Either of these routes enables the organism to salvage the degradation products of adenosine nucleotides, and recycle them back to nucleotide form.

Superpathways: superpathway of purine nucleotide salvage

Variants: adenine and adenosine salvage II, adenine and adenosine salvage III, adenine and adenosine salvage V, adenine and adenosine salvage VI, adenine salvage

Created 20-Jul-2000 by Pellegrini-Toole A, Marine Biological Laboratory
Revised 16-Sep-2010 by Caspi R, SRI International


Zannis78: Zannis V, Doyle D, Martin DW (1978). "Purification and characterization of human erythrocyte purine nucleoside phosphorylase and its subunits." J Biol Chem 253(2);504-10. PMID: 412851

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Alfonzo97: Alfonzo JD, Sahota A, Taylor MW (1997). "Purification and characterization of adenine phosphoribosyltransferase from Saccharomyces cerevisiae." Biochim Biophys Acta 1341(2);173-82. PMID: 9357956

Allen02: Allen M, Qin W, Moreau F, Moffatt B (2002). "Adenine phosphoribosyltransferase isoforms of Arabidopsis and their potential contributions to adenine and cytokinin metabolism." Physiol Plant 115(1);56-68. PMID: 12010467

Bennett03: Bennett EM, Li C, Allan PW, Parker WB, Ealick SE (2003). "Structural basis for substrate specificity of Escherichia coli purine nucleoside phosphorylase." J Biol Chem 278(47);47110-8. PMID: 12937174

BRENDA14: BRENDA team (2014). Imported from BRENDA version existing on Aug 2014.

Bzowska00: Bzowska A, Kulikowska E, Shugar D (2000). "Purine nucleoside phosphorylases: properties, functions, and clinical aspects." Pharmacol Ther 88(3);349-425. PMID: 11337031

Ealick90: Ealick SE, Rule SA, Carter DC, Greenhough TJ, Babu YS, Cook WJ, Habash J, Helliwell JR, Stoeckler JD, Parks RE (1990). "Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution." J Biol Chem 265(3);1812-20. PMID: 2104852

Guranowski79: Guranowski, Andrzej, Barankiewicz, Jerzy (1979). "Purine salvage in cotyledons of germinating lupin seeds." FEBS Letters 104(1): 95-98.

Hochstadt78a: Hochstadt J (1978). "Adenine phosphoribosyltransferase from Escherichia coli." Methods Enzymol 1978;51;558-67. PMID: 357906

HochstadtOzer71: Hochstadt-Ozer J, Stadtman ER (1971). "The regulation of purine utilization in bacteria. I. Purification of adenine phosphoribosyltransferase from Escherichia coli K12 and control of activity by nucleotides." J Biol Chem 246(17);5294-303. PMID: 4328693

Jensen75: Jensen KF, Nygaard P (1975). "Purine nucleoside phosphorylase from Escherichia coli and Salmonella typhimurium. Purification and some properties." Eur J Biochem 1975;51(1);253-65. PMID: 235429

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Lewis79: Lewis AS, Lowy BA (1979). "Human erythrocyte purine nucleoside phosphorylase: molecular weight and physical properties. A Theorell-Chance catalytic mechanism." J Biol Chem 254(19);9927-32. PMID: 114517

Pugmire02: Pugmire MJ, Ealick SE (2002). "Structural analyses reveal two distinct families of nucleoside phosphorylases." Biochem J 361(Pt 1);1-25. PMID: 11743878

Radabaugh02: Radabaugh TR, Sampayo-Reyes A, Zakharyan RA, Aposhian HV (2002). "Arsenate reductase II. Purine nucleoside phosphorylase in the presence of dihydrolipoic acid is a route for reduction of arsenate to arsenite in mammalian systems." Chem Res Toxicol 15(5);692-8. PMID: 12018991

Silva03: Silva RG, Carvalho LP, Oliveira JS, Pinto CA, Mendes MA, Palma MS, Basso LA, Santos DS (2003). "Cloning, overexpression, and purification of functional human purine nucleoside phosphorylase." Protein Expr Purif 27(1);158-64. PMID: 12509998

Sin72: Sin IL, Finch LR (1972). "Adenine phosphoribosyltransferase in Mycoplasma mycoides and Escherichia coli." J Bacteriol 112(1);439-44. PMID: 4562405

Stein81: Stein RL, Cordes EH (1981). "Kinetic alpha-deuterium isotope effects for Escherichia coli purine nucleoside phosphorylase-catalyzed phosphorolysis of adenosine and inosine." J Biol Chem 256(2);767-72. PMID: 6778874

Stoychev02: Stoychev G, Kierdaszuk B, Shugar D (2002). "Xanthosine and xanthine. Substrate properties with purine nucleoside phosphorylases, and relevance to other enzyme systems." Eur J Biochem 269(16);4048-57. PMID: 12180982

Williams84: Williams SR, Goddard JM, Martin DW (1984). "Human purine nucleoside phosphorylase cDNA sequence and genomic clone characterization." Nucleic Acids Res 12(14);5779-87. PMID: 6087295

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Sat Apr 30, 2016, biocyc13.