MetaCyc Pathway: adenine and adenosine salvage III
Inferred from experimentTraceable author statement to experimental support

Enzyme View:

Pathway diagram: adenine and adenosine salvage III

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: adenosine nucleotides salvage III

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

Some taxa known to possess this pathway include : Escherichia coli K-12 substr. MG1655, Halobacterium salinarum, Homo sapiens, Mycoplasma pneumoniae M129

Expected Taxonomic Range: Archaea, Bacteria , Eukaryota

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).

The distinction between nucleoside degradation and recycling is not always straight forward. This pathway shares several steps with the pathway adenosine nucleotides degradation II. However, this salvage pathway starts with adenine (which is often transported into the organism) and ends with IMP, leading to biosynthesis of nucleotides, while the degradation pathway starts with the nucleotide form ( AMP) and ends with urate, which in most organisms is degraded further.

A key enzyme in this pathway is adenosine deaminase, which converts adenosine to inosine. This has been shown to be the main form of adenosine degradation by the fungi Aspergillus terricola [Elshafei95] and Penicillium palitans [Elshafei05].

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

Unification Links: EcoCyc:PWY-6609

Created 21-Sep-2010 by Caspi R, SRI International


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

Elshafei05: Elshafei AM, Mohamed LA, Ali NH (2005). "Deamination of adenosine by extracts of Penicillium politans NRC-510." J Basic Microbiol 45(2);115-24. PMID: 15812856

Elshafei95: Elshafei AM, Abu-Shady MR, el-Beih FM, Mohamed LA (1995). "Mode and extent of degradation of adenosine and guanosine by extracts of Aspergillus terricola." Microbiol Res 150(3);291-5. PMID: 7551735

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

Ahmad68: Ahmad SI, Barth PT, Pritchard RH (1968). "Properties of a mutant of Escherichia coli lacking purine nucleoside phosphorylase." Biochim Biophys Acta 161(2);581-3. PMID: 4875425

Allen93a: Allen TE, Ullman B (1993). "Cloning and expression of the hypoxanthine-guanine phosphoribosyltransferase gene from Trypanosoma brucei." Nucleic Acids Res 21(23);5431-8. PMID: 8265360

Aono15: Aono R, Sato T, Imanaka T, Atomi H (2015). "A pentose bisphosphate pathway for nucleoside degradation in Archaea." Nat Chem Biol 11(5);355-60. PMID: 25822915

Balendiran99: Balendiran GK, Molina JA, Xu Y, Torres-Martinez J, Stevens R, Focia PJ, Eakin AE, Sacchettini JC, Craig SP (1999). "Ternary complex structure of human HGPRTase, PRPP, Mg2+, and the inhibitor HPP reveals the involvement of the flexible loop in substrate binding." Protein Sci 8(5);1023-31. PMID: 10338013

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

Bennett03a: Bennett EM, Anand R, Allan PW, Hassan AE, Hong JS, Levasseur DN, McPherson DT, Parker WB, Secrist JA, Sorscher EJ, Townes TM, Waud WR, Ealick SE (2003). "Designer gene therapy using an Escherichia coli purine nucleoside phosphorylase/prodrug system." Chem Biol 10(12);1173-81. PMID: 14700625

Bertosa14: Bertosa B, Mikleusevic G, Wielgus-Kutrowska B, Narczyk M, Hajnic M, Lescic Asler I, Tomic S, Luic M, Bzowska A (2014). "Homooligomerization is needed for stability: a molecular modelling and solution study of Escherichia coli purine nucleoside phosphorylase." FEBS J 281(7);1860-71. PMID: 24785777

Bezirdzhian86: Bezirdzhian KhO, Kocharian ShM, Akopian ZhI (1986). "[Isolation of the hexameric form of purine nucleoside phosphorylase from E. coli. Comparative study of trimeric and hexameric forms of the enzyme]." Biokhimiia 1986;51(7);1085-92. PMID: 3089333

Bezirdzhian87: Bezirdzhian KhO, Kocharian ShM, Akopian ZhI (1987). "[Hexamere purine nucleoside phosphorylase from Escherichia coli K-12. Kinetic analysis and mechanism of reaction]." Biokhimiia 52(11);1770-6. PMID: 3125860

Bezirdzhian87a: Bezirdzhian KhO, Kocharian ShM, Akopian ZhI (1987). "[Hexameric purine nucleoside phosphorylase II from Escherichia coli K-12. Physico-chemical and catalytic properties and stabilization with substrates]." Biokhimiia 1987;52(10);1624-31. PMID: 3122852

Bonthron85: Bonthron DT, Markham AF, Ginsburg D, Orkin SH (1985). "Identification of a point mutation in the adenosine deaminase gene responsible for immunodeficiency." J Clin Invest 76(2);894-7. PMID: 3839802

Buxton75: Buxton RS (1975). "Genetic analysis of thymidine-resistant and low-thymine-requiring mutants of Escherichia coli K-12 induced by bacteriophage Mu-1." J Bacteriol 121(2);475-84. PMID: 1089630

Buxton80: Buxton RS, Hammer-Jespersen K, Valentin-Hansen P (1980). "A second purine nucleoside phosphorylase in Escherichia coli K-12. I. Xanthosine phosphorylase regulatory mutants isolated as secondary-site revertants of a deoD mutant." Mol Gen Genet 179(2);331-40. PMID: 7007808

Bzowska88: Bzowska A, Kulikowska E, Darzynkiewicz E, Shugar D (1988). "Purine nucleoside phosphorylase. Structure-activity relationships for substrate and inhibitor properties of N-1-, N-7-, and C-8-substituted analogues; differentiation of mammalian and bacterial enzymes with N-1-methylinosine and guanosine." J Biol Chem 263(19);9212-7. PMID: 3132457

Bzowska92: Bzowska A, Kulikowska E, Shugar D (1992). "Formycins A and B and some analogues: selective inhibitors of bacterial (Escherichia coli) purine nucleoside phosphorylase." Biochim Biophys Acta 1120(3);239-47. PMID: 1576149

Chang91: Chang ZY, Nygaard P, Chinault AC, Kellems RE (1991). "Deduced amino acid sequence of Escherichia coli adenosine deaminase reveals evolutionarily conserved amino acid residues: implications for catalytic function." Biochemistry 30(8);2273-80. PMID: 1998686

Craig00: Craig SP, Eakin AE (2000). "Purine phosphoribosyltransferases." J Biol Chem 275(27);20231-4. PMID: 10816600

Daddona84: Daddona PE, Shewach DS, Kelley WN, Argos P, Markham AF, Orkin SH (1984). "Human adenosine deaminase. cDNA and complete primary amino acid sequence." J Biol Chem 259(19);12101-6. PMID: 6090454

Dandanell05: Dandanell G, Szczepanowski RH, Kierdaszuk B, Shugar D, Bochtler M (2005). "Escherichia coli purine nucleoside phosphorylase II, the product of the xapA gene." J Mol Biol 348(1);113-25. PMID: 15808857

Deo85: Deo SS, Tseng WC, Saini R, Coles RS, Athwal RS (1985). "Purification and characterization of Escherichia coli xanthine-guanine phosphoribosyltransferase produced by plasmid pSV2gpt." Biochim Biophys Acta 839(3);233-9. PMID: 3886014

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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