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Cd2+
-
with 0.2 mM, at 37°C, pH 7.4, 28% relative activity when compared to Co2+
Fe2+
-
with 0.2 mM, at 37°C, pH 7.4, 34% relative activity when compared to Co2+
MgCl2
-
most active at 0-0.2 mM, weak activity above 3 mM
Ca2+
-
requird for in Vitro tRNA processing reaction
Ca2+
-
optimal processing at 2 mM, nuclear RNase Z
Ca2+
-
optimal processing at 2 mM, nuclear RNase Z
Co2+
-
100% relative activity at 0.2 mM
Co2+
-
0.2 mM, no rescue of lost tRNase Z activity observed
Cu2+
-
with 0.2 mM, at 37°C, pH 7.4, 8% relative activity when compared to Co2+
Cu2+
-
0.2 mM, no rescue of lost tRNase Z activity observed
K+
-
optimum at 5 mM
K+
-
30 mM, mitochondrial RNase Z
Mg2+
-
2 mM, also required for in vitro tRNA processing reactions
Mg2+
Bacillus subtilis pre-tRNACys is cleaved in the presence of Mn2+ but not in the presence of Mg2+
Mg2+
-
highest reaction velocity at 0.3-1 mM
Mg2+
-
with 0.2 mM, at 37°C, pH 7.4, 54% relative activity when compared to Co2+. When the existing metal ion of the apoenzyme is removed with EDTA, with 0.2 mM, at 37°C, pH 7.4, 15% relative activity when compared to Co2+ after 60 min of incubation
Mg2+
-
5 mM, mitochondrial RNase Z
Mg2+
-
highest reaction velocity at 3 mM
Mg2+
-
10 mM, reaction kinetics indicated, cleavage by each variant in the presence of Mg2+ hardly detected, binding to pre-tRNA observed, essential for activity
Mg2+
-
5 mM, mitochondrial RNase Z
Mn2+
-
0.2 mM, addition of Mn2+ ions triples activity, also required for in Vitro tRNA processing reactions
Mn2+
Bacillus subtilis pre-tRNACys is cleaved in the presence of Mn2+ but not in the presence of Mg2+
Mn2+
-
with 0.2 mM, at 37°C, pH 7.4, 95% relative activity when compared to Co2+. When the existing metal ion of the apoenzyme is removed with EDTA, with 0.2 mM, at 37°C, pH 7.4, 23% relative activity when compared to Co2+ after 60 min of incubation
Mn2+
-
0.2 mM, reaction kinetics indicated, essential for activity, Mn2+ ions restore a lost Mg2+ dependent activity with two exceptions of the Asp52Ala and His222Ala substitutions
MnCl2
-
most active at 1-5 mM
MnCl2
-
most active at 0.05 mM
Zn2+
-
0.2 mM, addition of Zn2+ ions to the chelator-treated enzyme doubles activity, high affinity to Zn2+ even upon incubation with metal chelators, 0.76 Zn2+ ions retained per dimer
Zn2+
-
the catalytic core of monomer A contains two Zn2+
Zn2+
binding of two zinc ions coordinated by four residues in the signature His domain, catalytically important conserved contact between Glu231 and His24 shown
Zn2+
-
shows two fully loaded catalytic sites, which may result from Zn2+ addition during crystallization
Zn2+
-
with 0.2 mM, at 37°C, pH 7.4, 28% relative activity when compared to Co2+. When the existing metal ion of the apoenzyme is removed with EDTA, with 0.2 mM, at 37°C, pH 7.4, 26% relative activity when compared to Co2+ after 60 min of incubation
Zn2+
-
0.2 mM, no rescue of lost tRNase Z activity observed
Zn2+
-
part of active site, Zn1 ccoordinated with tetrahedral geometry and Zn2 coordinated with trigonal bipyramidal geometry, determined by crystallization
Zn2+
-
contains one Zn2+ ion per monomer
additional information
-
in contrast to bis(p-nitrophenyl)phosphate hydrolysis, pre-tRNA processing requires additional metal ions, Mn2+ or Mg2+, as Zn2+ ions alone are insufficient, metal dependence of the in vitro processing reaction analyzed, bis(p-nitrophenyl)phosphate activity of the chelator-treated AthTRZ1 without (TRZ-E) and with additional metal ions tested, chelator-treated AthTRZ1 without additional metal ions reveal same activity as the nonchelator-treated AthTRZ1
additional information
-
overview of the metal ion content in the active sites of tRNase Z and metallo-beta-lactamases, metal ion requirement by cleavage of bis(p-nitrophenyl)phosphate indicated, structure of metal binding site described, key residues of the zinc site identified by mutational studies summarized
additional information
-
metal binding sites in tRNase Z and metallo-beta-lactamases described
additional information
-
metal requirements, overview
additional information
-
metal requirements, overview