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MetaCyc Reaction: 3.1.3.5/3.1.3.v

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number: 3.1.3.5, 3.1.3.v

Enzymes and Genes:

Escherichia coli K-12 substr. MG1655: alkaline phosphataseInferred from experiment: phoA
purine nucleotidaseInferred from experiment: yrfG
UMP phosphatase: umpH
acid phosphatase / phosphotransferase: aphA
Homo sapiens: cytosolic 5'-nucleotidase IIInferred from experiment: NT5C2
5'-nucleotidase: NT5E
Saccharomyces cerevisiae: IMP-specific 5'-nucleotidaseInferred from experiment: ISN1
Solanum tuberosum: 5'-nucleotidaseInferred from experiment

In Pathway: adenosine nucleotides degradation I

Reaction Locations: cytosol, periplasm (sensu Gram-negative Bacteria)

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

Mass balance status: Balanced.

Enzyme Commission Primary Name for 3.1.3.5: 5′-nucleotidase

Enzyme Commission Synonyms for 3.1.3.5: uridine 5'-nucleotidase, 5'-adenylic phosphatase, adenosine 5'-phosphatase, AMP phosphatase, adenosine monophosphatase, 5'-mononucleotidase, AMPase, UMPase, snake venom 5'-nucleotidase, thimidine monophosphate nucleotidase, 5'-AMPase, 5'-AMP nucleotidase, AMP phosphohydrolase, IMP 5'-nucleotidase

Enzyme Commission Primary Name for 3.1.3.v: IMP-specific 5'-nucleotidase

Standard Gibbs Free Energy (ΔrG in kcal/mol): 7.2170105Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary for 3.1.3.5:
Wide specificity for 5-nucleotides.

Enzyme Commission Summary for 3.1.3.v:
The enzyme, isolated from the yeast Saccharomyces cerevisiae, is highly specific for IMP, and has no detectable activity with other purine and pyrimidine nucleotides. Requires divalent metals, such as Mg2+, Co2+ or Mn2+.

Citations: [Gulland38, Heppel51, Segal60, Itoh94, Itoh03]

Gene-Reaction Schematic

Gene-Reaction Schematic

Unification Links: KEGG:R01126, Rhea:27718

Relationship Links: BRENDA:EC:3.1.3.5, ENZYME:EC:3.1.3.5, IUBMB-ExplorEnz:EC:3.1.3.5


References

Gulland38: Gulland JM, Jackson EM (1938). "5-Nucleotidase." Biochem J 32(3);597-601. PMID: 16746659

Heppel51: Heppel LA, Hilmore RJ (1951). "Purification and properties of 5-nucleotidase." J Biol Chem 188(2);665-76. PMID: 14824154

Itoh03: Itoh R, Saint-Marc C, Chaignepain S, Katahira R, Schmitter JM, Daignan-Fornier B (2003). "The yeast ISN1 (YOR155c) gene encodes a new type of IMP-specific 5'-nucleotidase." BMC Biochem 4;4. PMID: 12735798

Itoh94: Itoh R (1994). "Purification and some properties of an IMP-specific 5'-nucleotidase from yeast." Biochem J 298 Pt 3;593-8. PMID: 8141771

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

Segal60: Segal HL, Brenner BM (1960). "5'-Nucleotidase of rat liver microsomes." J Biol Chem 235;471-4. PMID: 14444527


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 Sun May 1, 2016, biocyc14.