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Literature summary for 3.1.13.4 extracted from

  • Ren, Y.G.; Kirsebom, L.A.; Virtanen, A.
    Coordination of divalent metal ions in the active site of poly(A)-specific ribonuclease (2004), J. Biol. Chem., 279, 48702-48706.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
his-tagged recombinant wild type and mutants Escherichia coli

Protein Variants

Protein Variants Comment Organism
D28C mutants inactive in presence of Mg2+, but with restored activity in presence of soft divalent metal ions, amino acid interacts with catalytically essential metal ions Escherichia coli
D292C mutants inactive in presence of Mg2+, but with restored activity in presence of soft divalent metal ions, amino acid interacts with catalytically essential metal ions Escherichia coli
D382C mutants inactive in presence of Mg2+, but with restored activity in presence of soft divalent metal ions, amino acid interacts with catalytically essential metal ions Escherichia coli
E30C inactive mutant, acitivity cannot be restored Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Cd2+ 2 mM, activates reaction, can modulated the substrate length requirement Escherichia coli
Co2+ 2 mM, activates reaction, can modulated the substrate length requirement Escherichia coli
Mg2+ 2 mM, activates reaction, can modulated the substrate length requirement Escherichia coli
Mn2+ 2 mM, activates reaction Escherichia coli
Zn2+ 2 mM, activates reaction Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli BL21 (DE3)
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+ matrix Escherichia coli

Synonyms

Synonyms Comment Organism
PARN
-
Escherichia coli