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NaCl
-
activates at 50 mM, inhibits at concentrations above 100 mM
NH4Cl
-
activates at 50 mM, inhibits at concentrations above 100 mM
Co2+
activates
Co2+
-
can partially substitute for Mg2+
Co2+
can substitute for Mg2+
Co2+
-
can partially substitute for Mg2+ or Mn2+
Co2+
-
less effective than Mg2+
K+
-
-
K+
-
stimulates, maximum activity at 0.15-0.3 M
K+
-
stimulation at 20 mM
K+
-
maximum activity at 0.1 -0.15 M
KCl
-
activates at 50 mM, inhibits at concentrations above 100 mM
KCl
-
substrate affinity is enhanced under low-salt (10 mM KCl) conditions
KCl
KCl reduces the stability of Rnt1p/RNA complex
Mg2+
-
-
Mg2+
two Mg2+ ions are required for the cleavage of each phosphodiester bond
Mg2+
-
required, Mg2+ and Mn2+ both support the catalytic reaction
Mg2+
-
divalent metal ion requirement for catalysis
Mg2+
-
divalent metal ion requirement for catalysis
Mg2+
-
divalent metal ion requirement for catalysis
Mg2+
-
higher requirement in G97E mtuants
Mg2+
-
different cleavage pattern depending on the cation used
Mg2+
-
activity with recombinant hybrid enzyme mutants, overview
Mg2+
-
dependent on, optimal at 25 mM
Mg2+
-
divalent metal ion requirement for catalysis
Mg2+
-
divalent metal required, Mg2+ is the preffered species, evidennce for involvement of two Mg2+ ions in phosphodiester hydrolysis
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
Mg2+
essential for catalysis, two Mg2+ ions in the catalytic site, and a third Mg2+ ion, which has been proposed to be involved in product release, binding structure, overview
Mg2+
essentially required for activity
Mg2+
RNase III requires two transition metal ions to stabilize the catalytic valley where it cleaves dsRNA. Mg2+ is the most favored metal ion in the case of Escherichia coli RNase III. Two Mg2+ ions interact with negatively charged amino acids and form a hydrogen bond with nucleotide residues of cleavage sites within each catalytic site
Mg2+
-
divalent metal ion requirement for catalysis
Mg2+
two ions bound around the active site, one of which is involved in the catalytic mechanism and the second in RNA substrate binding
Mg2+
Paramecium bursaria Chlorella virus-1
-
dependent on, optimum concentration is about 5 mM
Mg2+
-
activity with recombinant hybrid enzyme mutants, overview
Mg2+
dsRNA substrate is cleaved by the RBIV RNase III at high concentrations of Mg2+ (5-20 mM) and at low salt concentration (50 mM)
Mg2+
-
recombinant Sa-RNase III requires MgCl2 for activity
Mg2+
-
Mg2+ best supports the catalytic activity of enzyme RNase3
Mg2+
-
activates optimally at 1 mM
Mn2+
-
-
Mn2+
-
required, Mg2+ and Mn2+ both support the catalytic reaction
Mn2+
-
can partially substitute for Mg2+
Mn2+
can substitute for Mg2+
Mn2+
-
different cleavage pattern depending on the cation used
Mn2+
-
optimal concentration at 0.15-0.3 mM
Mn2+
-
activity with recombinant hybrid enzyme mutants, overview
Mn2+
-
can substitute for Mg2+ in vitro, at 5 mM
Mn2+
-
can substitute for Mg2+, showing slightly higher activity with the wild-type enzyme, highly activates the mutant E117D, no activity with mutant E117Q
Mn2+
-
divalent metal required, Mn2+ can replace Mg2+ in activation
Mn2+
Paramecium bursaria Chlorella virus-1
-
can substitute for Mg2+, best at 1 mM, leads to production of additional cleavage products
Mn2+
-
activity with recombinant hybrid enzyme mutants, overview
Mn2+
substrate dsRNA is cleaved at low concentrations of Mn2+ (0.5-1 mM) at low salt concentration (50 mM) and is cleaved by increasing Mn2+ (5-20 mM) at 200 mM salt
Mn2+
activates, required, best metal ion at 0.1-50 mM, inhibitory at 100 mM
Mn2+
-
less efficient in activation of the enzyme compared to Mg2+, but binding of 21 nt small dsRNA molecules is most efficient in the presence of Mn2+
Mn2+
-
less effective than Mg2+
Na+
-
required
Na+
-
stimulates, maximum activity at 0.15-0.3 M
Na+
-
stimualtion at 20 mM
Ni2+
activates
Ni2+
-
can partially substitute for Mg2+
Ni2+
can substitute for Mg2+
Ni2+
-
can partially substitute for Mg2+ or Mn2+
Ni2+
-
less effective than Mg2+
Zn2+
-
inhibits Mg2+ dependent reaction
Zn2+
-
less efficient in activation of the enzyme compared to Mg2+
additional information
-
no activation by Ni2+, Co2+, and Ca2+
additional information
no activation by Ca2+. The enzyme requires a divalent metal ion for catalysis, catalysis appears to be largely driven by the two metals. The adjacency of the two metal ions and their interaction with the scissile phosphodiester linkage fit the well-studied two-metal-ion catalytic mechanism, wherein one metal binds and activates the water nucleophile, and the second metal facilitates departure of the 3'-oxygen atom. Both metal ions are jointly coordinated to the side chain of a highly conserved, functionally essential glutamic acid E110
additional information
RNase III requires two transition metal ions to stabilize the catalytic valley where it cleaves dsRNAI
additional information
-
cleavage activity of Bm-RNase III is bivalent metal cations-dependent
additional information
-
metal ion specificity of the enzyme is determined by the N-terminus
additional information
-
no activity of mutant E117Q with Ca2+, Ni2+, Co2+, or Sr2+
additional information
-
no activity with Ca2+ and Sr2+
additional information
-
no activation by Ca2+. The enzyme requires a divalent metal ion for catalysis, catalysis appears to be largely driven by the two metals. The adjacency of the two metal ions and their interaction with the scissile phosphodiester linkage fit the well-studied two-metal-ion catalytic mechanism, wherein one metal binds and activates the water nucleophile, and the second metal facilitates departure of the 3'-oxygen atom. Both metal ions are jointly coordinated to the side chain of a highly conserved, functionally essential glutamic acid E117
additional information
while Mn2+, Ni2+, and Co2+ can also support the catalytic activity of RNase III in vitro, extracellular levels of Ni2+ and Co2+ do not significantly alter RNase III activity
additional information
-
while Mn2+, Ni2+, and Co2+ can also support the catalytic activity of RNase III in vitro, extracellular levels of Ni2+ and Co2+ do not significantly alter RNase III activity
additional information
the enzyme requires a divalent metal ion for catalysis
additional information
-
the enzyme requires a divalent metal ion for catalysis
additional information
the enzyme requires a divalent metal ion for catalysis
additional information
the enzyme recognizes RNA motifs and cleaves substrates at specific sites in a divalent-metal-ion-dependent manner. The RNA cleavage activity of the enzyme can be supported by Mg2+, Mn2+, and Co2+ and enhanced with the increasing salt concentration. BCGRNase III can exploit Mg2+, Mn2+, and Co2+, but not Ni2+, Ca2+, Zn2+, and Cu2+, as a cofactors to show RNA cleavage activity. The maximum activity of the enzyme supported by Mn2+ ions is 0.12fold higher than that supported by Mg2+ ions
additional information
-
metal ion specificity of the enzyme is determined by the N-terminus
additional information
-
the enzyme requires a divalent metal ion for catalysis
additional information
-
the enzyme requires a divalent metal ion for catalysis
additional information
Ca2+ does not likely support enzyme activity. Strictly metal cofactor-dependent activity of SmRNase III on the model R1.1 substrate
additional information
-
Ca2+ does not likely support enzyme activity. Strictly metal cofactor-dependent activity of SmRNase III on the model R1.1 substrate
additional information
-
no activation of the enzyme by Ca2+
additional information
-
the enzyme functions optimally at pH 8 and about 50-80 mM salt concentrations
additional information
the enzyme requires a divalent metal ion for catalysis
additional information
-
recombinant mRPN1 requires Mg2+ and a critical catalytic carboxylate