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Literature summary for 3.1.26.3 extracted from

  • Sun, W.; Li, G.; Nicholson, A.W.
    Mutational analysis of the nuclease domain of Escherichia coli ribonuclease III. Identification of conserved acidic residues that are important for catalytic function in vitro (2004), Biochemistry, 43, 13054-13062.
    View publication on PubMed
Search for more literature for 3.1.26.3

Cloned(Commentary)

Cloned (Comment) Organism
mutant proteins expressed in Escherichia coli Escherichia coli

Protein Variants

Protein Variants Comment Organism
D114A mutant exhibits catalytic activity in vitro in 10 mM Mg2+ buffer that is comparable to that of the wild-type enzyme. At 1 mM Mg2+, the activity is significantly lower, KM-value for Mg2+ is about 2.8fold larger than the wild-type value Escherichia coli
D45A mutant enzyme exhibits negligible activity, regardless of the Mg2+ concentration Escherichia coli
D45E activity is partially rescued by Mn2+ Escherichia coli
D45E mutant enzyme exhibits negligible activity, regardless of the Mg2+ concentration Escherichia coli
D45N mutant enzyme exhibits negligible activity, regardless of the Mg2+ concentration Escherichia coli
E100A mutant enzyme requires higher Mg2+ concentrations for optimal activity than the wild-type enzyme Escherichia coli
E38A mutant enzyme requires higher Mg2+ concentrations for optimal activity than the wild-type enzyme Escherichia coli
E41A mutant exhibits catalytic activity in vitro in 10 mM Mg2+ buffer that is comparable to that of the wild-type enzyme. At 1 mM Mg2+, the activity is significantly lower, KM-value for Mg2+ is about 2.8fold larger than the wild-type value Escherichia coli
E41A/D114A KM-value for Mg2+ is about 85fold larger than the wild-type value Escherichia coli
E65A mutant enzyme requires higher Mg2+ concentrations for optimal activity than the wild-type enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000041
-
 R1.1 RNA pH 7.5, 37°C, buffer containing 10 mM Mg2+, mutant enzyme E41A Escherichia coli
0.000054
-
 R1.1 RNA pH 7.5, 37°C, buffer containing 10 mM Mg2+, mutant enzyme E38A Escherichia coli
0.000056
-
 R1.1 RNA pH 7.5, 37°C, buffer containing 10 mM Mg2+, mutant enzyme E65A Escherichia coli
0.000066
-
 R1.1 RNA pH 7.5, 37°C, buffer containing 10 mM Mg2+, wild-type enzyme Escherichia coli
0.000071
-
 R1.1 RNA pH 7.5, 37°C, buffer containing 10 mM Mg2+, mutant enzyme D114A Escherichia coli
0.000544
-
 R1.1 RNA pH 7.5, 37°C, buffer containing 10 mM Mg2+, mutant enzyme E100A Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, K(Mg2+): 0.46 mM for wild-type enzyme, 1.58 mM for mutant enzyme E38A, 1.25 mM for mutant enzyme E41A, 1.27 mM for mutant enzyme E65A, 2.48 mM for mutant enzyme E100A, 1.35 mM for mutant enzyme D114A, 39 mM for mutant enzyme E41A/D114A Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant mutant enzymes Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
R1.1 RNA + H2O
-
 Escherichia coli ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.032
-
 R1.1 RNA pH 7.5, 37°C, buffer containing 10 mM Mg2+, mutant enzyme E41A Escherichia coli
0.09
-
 R1.1 RNA pH 7.5, 37°C, buffer containing 10 mM Mg2+, mutant enzyme E38A Escherichia coli
0.098
-
 R1.1 RNA pH 7.5, 37°C, buffer containing 10 mM Mg2+, mutant enzyme E65A Escherichia coli
0.14
-
 R1.1 RNA pH 7.5, 37°C, buffer containing 10 mM Mg2+, wild-type enzyme Escherichia coli
0.165
-
 R1.1 RNA pH 7.5, 37°C, buffer containing 10 mM Mg2+, mutant enzyme D114A Escherichia coli
0.72
-
 R1.1 RNA pH 7.5, 37°C, buffer containing 10 mM Mg2+, mutant enzyme E100A Escherichia coli