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Literature summary extracted from

  • Wallden, K.; Nordlund, P.
    Structural basis for the allosteric regulation and substrate recognition of human cytosolic 5-nucleotidase II (2011), J. Mol. Biol., 408, 684-696.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.3.5 2,3-bisphosphoglycerate allosteric activation Homo sapiens
3.1.3.5 ATP allosteric activation Homo sapiens
3.1.3.5 diadenosine polyphosphate allosteric activation Homo sapiens
3.1.3.5 additional information structural basis for the allosteric activation of cN-II via a mechanism where an effector-induced disorder-to-order transition generates rearrangements within the catalytic site and the subsequent coordination of the catalytically essential magnesium. Central to the activation is the large transition of the catalytically essential Asp356. Neither substrate nor Mg2+ bound to this form, supporting an allosteric mechanism in which effector-induced conformational changes are required to increase the affinity for Mg2+ and the substrate Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.5 expression of mutant D52N in Escherichia coli strain BL21(DE)-R3-pRARE2 Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.3.5 analysis of crystal structures of the inactive D52N mutant enzyme in apoform or in complexes with 1. 2,3-bisphosphoglycerate, 2. IMP/ATP, 3. IMP/2,3-bisphosphoglycerate, 4. GMP/diadenosine tetraphosphate, 5. dGMP/dATP, or 6. UMP/ATP, overview. Crystallization by sitting drop vapor diffusion method with sitting drops of 300 nl at a protein solution/reservoir solution ratio of 2:1, the reservoir solution contains 0.1 M bicine, pH 9.0, and 10% w/v PEG 6000, with 20 mM MgCl2, 10 mM dATP, and 10 mM dGMP added to the protein solution, 7.7 mg/ml protein, 1-2 weeks at 4°C, to obtain the enzyme complexes the crystals are soaked in 0.01 ml drops of reservoir solution supplemented with 10 mM of the corresponding substrate/activator and 20 mM MgCl2 for 90 min, X-ray diffraction structure determination and analysis at A resolution Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.5 D52N site-directed mutagenesis, catalytically inactive active site residue Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.3.5 cytosol
-
 Homo sapiens 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.5 Mg2+ required, catalytically essential Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.5 additional information Homo sapiens cytosolic 5'-nucleotidase II catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.5 Homo sapiens P49902
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.5 5'-AMP + H2O
-
 Homo sapiens adenosine + phosphate
-
 ?
3.1.3.5 5'-dGMP + H2O
-
 Homo sapiens deoxyguanosine + phosphate
-
 ?
3.1.3.5 5'-GMP + H2O
-
 Homo sapiens guanosine + phosphate
-
 ?
3.1.3.5 5'-IMP + H2O
-
 Homo sapiens inosine + phosphate
-
 ?
3.1.3.5 5'-UMP + H2O
-
 Homo sapiens uridine + phosphate
-
 ?
3.1.3.5 additional information cytosolic 5'-nucleotidase II catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates Homo sapiens ?
-
 ?
3.1.3.5 additional information structural basis for the substrate specificity of cN-II: Arg202, Asp206, and Phe157 seem to be important residues for purine/pyrimidine selectivity Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.3.5 More cN-II is a relatively large enzyme of the structural HAD superfamily, which contains, besides the alpha/beta-Rossmann fold and the four-helix bundle, non-conserved regions involved in effector binding and subunit-subunit interactions Homo sapiens
3.1.3.5 tetramer cN-II functions as a tetramer forming a dimer of dimers, structural basis for the allosteric regulation and substrate recognition of cytosolic 5-nucleotidase II, overview. The effector binding site, corresponding to effector site 1, is located close to one of the subunit interfaces where the effector takes part in subunit-subunit interactions by forming electrostatic interactions between the effector phosphates and the positively charged residues of each subunit Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.1.3.5 cN-II
-
 Homo sapiens
3.1.3.5 cytosolic 5'-nucleotidase II
-
 Homo sapiens
3.1.3.5 More cN-II is a relatively large enzyme of the structural HAD superfamily Homo sapiens

General Information

EC Number General Information Comment Organism
3.1.3.5 metabolism the nucleotide salvage pathway is regulated at a molecular level Homo sapiens
3.1.3.5 additional information the enzyme interferes with the phosphorylation-dependent activation of nucleoside analogues used in the treatment of cancer and viral diseases Homo sapiens
3.1.3.5 physiological function cytosolic 5'-nucleotidase II catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates and participates in the regulation of purine nucleotide pools within the cell Homo sapiens