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Literature summary for 3.1.13.4 extracted from

  • Martinez, J.; Ren, Y.G.; Thuresson, A.C.; Hellman, U.; Astrom, J.; Virtanen, A.
    A 54-kDa fragment of the Poly(A)-specific ribonuclease is an oligomeric, processive, and cap-interacting Poly(A)-specific 3' exonuclease (2000), J. Biol. Chem., 275, 24222-24230.
    View publication on PubMed
Search for more literature for 3.1.13.4

Inhibitors

Inhibitors Comment Organism Structure
m7G(5')ppp(5')G cap analogue
-
 Bos taurus

Metals/Ions

Metals/Ions Comment Organism Structure
K+ required, optimal around 100 mM Bos taurus
Mg2+ divalent cation required around 1 mM, Mg2+ being most effective Bos taurus
Mn2+ may partly substitute for Mg2+, 17% of activity detected with Mg2+ Bos taurus
additional information no activtiy with Zn2+, Ca2+ Bos taurus
Na+ may substitute for K*, less effective Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
74000
-
 3 * 74000, SDS-PAGE, a 54000 Da polypeptide fragment is responsible for activity Bos taurus
180000 220000 gel filtration Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
 enzyme and 54 kDa fragment of enzyme
-

Purification (Commentary)

Purification (Comment) Organism
partial Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
thymus
-
 Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
211000
-
 pH 7.0, 30°C Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
poly(A)-mRNA + H2O
-
 Bos taurus 5'-AMP
-
 ?

Subunits

Subunits Comment Organism
trimer 3 * 74000, SDS-PAGE, a 54000 Da polypeptide fragment is responsible for activity Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Bos taurus