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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | O95453 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | active site structure, modelling, overview | Homo sapiens | ? | - |
? |
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 | 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 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 | 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 |