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Literature summary for 3.1.13.4 extracted from

  • He, G.J.; Liu, W.F.; Yan, Y.B.
    Dissimilar roles of the four conserved acidic residues in the thermal stability of poly(a)-specific ribonuclease (2011), Int. J. Mol. Sci., 12, 2901-2916.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
D28A site-directed mutagenesis, structure comparison to the wild-type enzyme, the mutant shows unaltered ellipticity Homo sapiens
D292A site-directed mutagenesis, structure comparison to the wild-type enzyme, the mutant shows unaltered ellipticity Homo sapiens
D382A site-directed mutagenesis, structure comparison to the wild-type enzyme, the mutant shows slightly decreased ellipticity Homo sapiens
E30A site-directed mutagenesis, structure comparison to the wild-type enzyme, the mutant shows significantly decreased ellipticity Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, the active site of PARN contains four conserved acidic amino acid residues, D28, E30, D292 and D382, the latter being the most important, that coordinate two Mg2+ ions and are essential for the catalytic activity. These acidic residues form a negative charge cave that can bind with two Mg2+ ions. Cofactor Mg2+ is also important to PARN stability against inactivation induced by heat treatment, but promotes thermal aggregation at high temperatures. Mg2+ significantly decreases the rate but increases the aggregate size of the 54 kDa wild-type enzyme in a concentration-dependent manner. The metal cofactor binding or mutation induces changes in the microenvironments around Trp residues Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O95453
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information active site structure, modelling, overview Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
More the full length PARN enzyme contains three well-defined domains: the catalytic domain, the R3H domain, and the RNA-recognition motif, RRM Homo sapiens

Synonyms

Synonyms Comment Organism
More poly(A)-specific ribonuclease belongs to the DEDD superfamily of 3'-exonucleases Homo sapiens
PARN
-
Homo sapiens
poly(A)-specific ribonuclease
-
Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45 55 thermal stability and aggregation kinetic parameters, the aggregation is dominated by a first-order kinetics, increase in t0 and the decrease in k implies that Mg2+ can inhibit the rate of enzyme aggregation, overview. Cofactor Mg2+ is also important to PARN stability against inactivation induced by heat treatment, but promotes thermal aggregation at high temperatures. Mg2+ significantly decreases the rate but increases the aggregate size of the 54 kDa wild-type enzyme in a concentration-dependent manner. Effect of mutations on the Mg2+-dependent enzyme thermal aggregation, overview Homo sapiens

General Information

General Information Comment Organism
additional information alterations in the active site structure by metal binding or mutations might lead to a global conformational change of the enzyme PARN molecule Homo sapiens
physiological function poly(A)-specific ribonuclease is involved in the mRNA decay regulation by specifically catalyzing the shortening of the 3'-end poly(A) tail Homo sapiens