Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.13.4 extracted from

  • He, G.J.; Zhang, A.; Liu, W.F.; Yan, Y.B.
    Distinct roles of the R3H and RRM domains in poly(A)-specific ribonuclease structural integrity and catalysis (2013), Biochim. Biophys. Acta, 1834, 1089-1098.
    View publication on PubMed
Search for more literature for 3.1.13.4

Cloned(Commentary)

Cloned (Comment) Organism
-
 Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information construction of deletion mutants, i.e. expression of the N-terminal fragment residues 1-540, the N-terminal fragment residues 1­-520, the N-terminal fragment residues 1-470, the N-terminal fragment residues 1-446, residues 1-520 with the deletion of the R3H domain, residues 1-446 with the deletion of the R3H domain. N-terminal fragment residues 1-446, residues 1-520 with the deletion of the R3H domain, residues 1-446 with the deletion of the R3H domain display 30.9%, 5.9% and 2.5% of the catalytic efficiency of the N-terminal fragment residues 1-520, respectively Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O95453
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(A)6 + H2O
-
 Homo sapiens 5'-AMP + ?
-
 ?
poly(A) + H2O average substrate length about 200 A Homo sapiens 5'-AMP + ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.65
-
 Poly(A) residues 1-446 with the deletion of the R3H domain, pH 7.0, temperature not specified in the publication Homo sapiens
1.1
-
 Poly(A) residues 1-520 with the deletion of the R3H domain, pH 7.0, temperature not specified in the publication Homo sapiens
5.6
-
 Poly(A) N-terminal fragment residues 1-446, pH 7.0, temperature not specified in the publication Homo sapiens
7.6
-
 Poly(A) N-terminal fragment residues 1-520, pH 7.0, temperature not specified in the publication Homo sapiens

General Information

General Information Comment Organism
physiological function the R3H domain has the ability to bind various oligonucleotides at the micromolar level with no oligo(A) specificity. The removal of the R3H domain dissociates poly(A)-specific ribonuclease into monomers, which still possess the RNA-binding ability and catalytic functions. The removal of the R3H domain does not affect the catalytic pattern of poly(A)-specific ribonuclease. Both R3H domain and RNA-recognition motif domain RRM may be essential for the high affinity of long poly(A) substrate, but the R3H domain does not contribute to the substrate recognition. Compared to the RRM domain, the R3H domain plays a more important role in the structural integrity of the dimeric poly(A)-specific ribonuclease Homo sapiens