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MetaCyc Pathway: adenosine nucleotides degradation III
Inferred from experiment

Enzyme View:

Pathway diagram: adenosine nucleotides degradation 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 ribonucleotide/ribonucleoside metabolism

Superclasses: Degradation/Utilization/AssimilationNucleosides and Nucleotides DegradationPurine Nucleotides DegradationAdenosine Nucleotides Degradation

Some taxa known to possess this pathway include : Azotobacter vinelandii, Escherichia coli K-12 substr. MG1655

Expected Taxonomic Range: Bacteria

General Background

The distinction between nucleoside degradation and salvage is not always straight forward. A general rule is that degradation pathways start with the nucleotide forms and convert them to simpler forms, eventually leading to complete mineralization, while salvage pathways start with either the nucleoside or the free base form, and convert those to the nucleotide forms.

Nucleotide recycling is achieved by a combination of both types - a nucleotide is partially degraded via a degradation pathway, but the products are shuttled into a salvage pathway rather then towrds complete mineralization.

About This Pathway

The pathway that is described here is a degradation pathway found in some bacteria, that typically feeds into a salvage pathway. In Escherichia coli K-12 this is the major route of AMP catabolism. AMP degradation is not used necessarily for energy production, but is often required for maintaining the ATP to AMP ratio at relatively constant levels in the face of declining absolute levels of ATP. Thus partial degradation of AMP to a product that can be recycled to the nucleotide later is desired.

The enzyme AMP nucleosidase ( EC Can convert AMP into adenine in a single step [Leung80]. The adenine that is produced in the nucleosidase reaction can be reincorporated into the purine pool via the salvage pathways [Leung80, Leung89].

Variants: adenosine nucleotides degradation I, adenosine nucleotides degradation II, adenosine nucleotides degradation IV

Unification Links: EcoCyc:PWY-6617

Created 27-Sep-2010 by Caspi R, SRI International


Leung80: Leung HB, Schramm VL (1980). "Adenylate degradation in Escherichia coli. The role of AMP nucleosidase and properties of the purified enzyme." J Biol Chem 1980;255(22);10867-74. PMID: 7000783

Leung89: Leung HB, Kvalnes-Krick KL, Meyer SL, deRiel JK, Schramm VL (1989). "Structure and regulation of the AMP nucleosidase gene (amn) from Escherichia coli." Biochemistry 1989;28(22);8726-33. PMID: 2690948

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

Baek06: Baek JH, Lee SY (2006). "Novel gene members in the Pho regulon of Escherichia coli." FEMS Microbiol Lett 264(1);104-9. PMID: 17020555

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

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Giranda89: Giranda VL, Berman HM, Schramm VL (1989). "Crystallographic quaternary structural analysis of AMP nucleosidases from Escherichia coli and Azotobacter vinelandii." J Biol Chem 264(26);15674-80. PMID: 2670945

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

KvalnesKrick93: Kvalnes-Krick K, Labdon JE, Ma X, Nieves E, Schramm VL (1993). "Mutagenic analysis of AMP nucleosidase from Escherichia coli. Deletion of a region similar to AMP deaminase and peptide characterization by mass spectrometry." J Biol Chem 268(12);8717-26. PMID: 8473316

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

Leung84: Leung HB, Schramm VL (1984). "The structural gene for AMP nucleosidase. Mapping, cloning, and overproduction of the enzyme." J Biol Chem 259(11);6972-8. PMID: 6327703

Morrison08: Morrison BA, Shain DH (2008). "An AMP nucleosidase gene knockout in Escherichia coli elevates intracellular ATP levels and increases cold tolerance." Biol Lett 4(1);53-6. PMID: 18029299

Mushegian94: Mushegian AR, Koonin EV (1994). "Unexpected sequence similarity between nucleosidases and phosphoribosyltransferases of different specificity." Protein Sci 3(7);1081-8. PMID: 7920254

Parkin84: Parkin DW, Schramm VL (1984). "Effects of allosteric activation on the primary and secondary kinetic isotope effects for three AMP nucleosidases." J Biol Chem 259(15);9418-25. PMID: 6378909

Parkin87: Parkin DW, Schramm VL (1987). "Catalytic and allosteric mechanism of AMP nucleosidase from primary, beta-secondary, and multiple heavy atom kinetic isotope effects." Biochemistry 26(3);913-20. PMID: 3552037

Parkin91: Parkin DW, Mentch F, Banks GA, Horenstein BA, Schramm VL (1991). "Transition-state analysis of a Vmax mutant of AMP nucleosidase by the application of heavy-atom kinetic isotope effects." Biochemistry 30(18);4586-94. PMID: 2021651

Parry11: Parry BR, Shain DH (2011). "Manipulations of AMP metabolic genes increase growth rate and cold tolerance in Escherichia coli: implications for psychrophilic evolution." Mol Biol Evol 28(7);2139-45. PMID: 21300985

Schramm78: Schramm VL, Leung HB (1978). "Adenosine monophosphate nucleosidase from Azotobacter vinelandii and Escherichia coli." Methods Enzymol 1978;51;263-70. PMID: 357895

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Zhang04e: Zhang Y, Cottet SE, Ealick SE (2004). "Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases." Structure (Camb) 12(8);1383-94. PMID: 15296732

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 Fri Apr 29, 2016, biocyc13.