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bis(p-nitrophenyl)phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
pre-tRNA + H2O
?
-
the glycine/proline-rich ZiPD exosite of tRNase Z takes part in the pre-tRNA binding, it is a flexible arm which protrudes from the main protein body
-
-
?
thymidine 5'-p-nitrophenyl phosphate + H2O
p-nitrophenol + TMP
-
-
-
-
?
thymidine-5-p-nitrophenyl phosphate + H2O
p-nitrophenol + TMP
-
TpNPP substrate, phosphodiesterase activities of tRNase Z on small chromogenic substrates mentioned, structural features of potential model substrates indicated
-
-
?
usRNA1 + H2O
?
-
24 nt unstructured RNA
-
-
?
usRNA10 + H2O
?
-
40 nt unstructured RNA
-
-
?
usRNA2 + H2O
?
-
24 nt unstructured RNA
-
-
?
usRNA3 + H2O
?
-
28 nt unstructured RNA
-
-
?
usRNA4 + H2O
?
-
39 nt unstructured RNA
-
-
?
usRNA5 + H2O
?
-
26 nt unstructured RNA
-
-
?
usRNA6 + H2O
?
-
26 nt unstructured RNA
-
-
?
usRNA7 + H2O
?
-
24 nt unstructured RNA
-
-
?
usRNA8 + H2O
?
-
43 nt unstructured RNA
-
-
?
usRNA9 + H2O
?
-
22 nt unstructured RNA
-
-
?
additional information
?
-
bis(p-nitrophenyl)phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
-
bpNPP substrate, phosphodiesterase activities of tRNase Z on small chromogenic substrates mentioned, structural features of potential model substrates indicated
-
-
?
bis(p-nitrophenyl)phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
-
evidences for sigmoidal saturation kinetics with the small chromogenic phosphodiester substrate reviewed
-
-
?
bis(p-nitrophenyl)phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
-
displays efficient phosphodiesterase activity against bis(p-nitrophenyl) phosphate, which is unusual among the RNase Z family of enzymes
-
-
?
bis(p-nitrophenyl)phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
-
phosphodiesterase activity
-
-
?
additional information
?
-
-
involvement of tRNase Z in mRNA processing
-
-
?
additional information
?
-
-
RNase BN is active on both double- and single-stranded RNA but duplex RNA is preferred. Displays a profound base specificity, showing no activity on runs of C residues. Digestion by RNase BN leads to 3-mers as the limit products, but the rate slows on molecules shorter than 10 nucleotides in length. RNase BN acts as a distributive exoribonuclease on some substrates, releasing mononucleotides and a ladder of digestion products. RNase BN also cleaves endonucleolytically, releasing 3' fragments as short as 4 nucleotides
-
-
?
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Cd2+
-
with 0.2 mM, at 37°C, pH 7.4, 28% relative activity when compared to Co2+
Co2+
-
100% relative activity at 0.2 mM
Cu2+
-
with 0.2 mM, at 37°C, pH 7.4, 8% relative activity when compared to Co2+
Fe2+
-
with 0.2 mM, at 37°C, pH 7.4, 34% relative activity when compared to Co2+
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
Mg2+
-
required
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
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
additional information
-
metal binding sites in tRNase Z and metallo-beta-lactamases described
additional information
-
metal requirements, overview
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Shibata, H.S.; Minagawa, A.; Takaku, H.; Takagi, M.; Nashimoto, M.
Unstructured RNA is a substrate for tRNase Z
Biochemistry
45
5486-5492
2006
Bacillus subtilis, Escherichia coli, Homo sapiens, Pyrobaculum aerophilum, Saccharomyces cerevisiae, Sus scrofa, Thermotoga maritima
brenda
Vogel, A.; Schilling, O.; Spath, B.; Marchfelder, A.
The tRNase Z family of proteins: physiological functions, substrate specificity and structural properties
Biol. Chem.
386
1253-1264
2005
Arabidopsis thaliana, Arabidopsis thaliana (Q8L633), Arabidopsis thaliana (Q8LGU7), Arabidopsis thaliana (Q8VYS2), Bacillus subtilis (P54548), Caenorhabditis elegans (O44476), Drosophila melanogaster (Q8MKW7), Escherichia coli (P0A8V0), Haloferax volcanii, Homo sapiens (Q9BQ52), Homo sapiens (Q9H777), Methanocaldococcus jannaschii (Q58897), Pyrobaculum aerophilum (Q8ZTJ7), Pyrococcus furiosus (Q8U182), Saccharomyces cerevisiae (P36159), Thermoplasma acidophilum (Q9HJ19), Thermotoga maritima
brenda
Kostelecky, B.; Pohl, E.; Vogel, A.; Schilling, O.; Meyer-Klaucke, W.
The crystal structure of the zinc phosphodiesterase from Escherichia coli provides insight into function and cooperativity of tRNase Z-family proteins
J. Bacteriol.
188
1607-1614
2006
Escherichia coli
brenda
Dominski, Z.
Nucleases of the metallo-beta-lactamase family and their role in DNA and RNA metabolism
Crit. Rev. Biochem. Mol. Biol.
42
67-93
2007
Escherichia coli, Homo sapiens
brenda
Redko, Y.; Li de Lasierra-Gallay, I.; Condon, C.
When alls zed and done: the structure and function of RNase Z in prokaryotes
Nat. Rev. Microbiol.
5
278-286
2007
Aspergillus nidulans, Bacillus subtilis (P54548), Bacteroides fragilis, Bombyx mori, Bradyrhizobium japonicum, Caenorhabditis elegans, Chlamydia trachomatis, Clostridium acetobutylicum, Clostridium spp., Deinococcus radiodurans, Drosophila melanogaster, Escherichia coli, Haloquadratum walsbyi, Lacticaseibacillus casei, Listeria monocytogenes, Methanocaldococcus jannaschii, Methanococcoides burtonii, Mycobacterium tuberculosis, Myxococcus xanthus, Nanoarchaeum equitans, Prochlorococcus marinus, Saccharolobus solfataricus, Saccharomyces cerevisiae, Staphylococcus aureus, Streptococcus pneumoniae, Streptomyces coelicolor, Thermotoga maritima, Treponema pallidum, Xenopus laevis
brenda
Ceballos, M.; Vioque, A.
tRNase Z
Protein Pept. Lett.
14
137-145
2007
Synechocystis sp., Arabidopsis thaliana, Bacillus subtilis, Escherichia coli, Homo sapiens, Methanocaldococcus jannaschii, Thermotoga maritima
brenda
Elbarbary, R.A.; Takaku, H.; Nashimoto, M.
Functional analyses for tRNase Z variants: an aspartate and a histidine in the active site are essential for the catalytic activity
Biochim. Biophys. Acta
1784
2079-2085
2008
Bacillus subtilis, Escherichia coli, Homo sapiens, Mus musculus
brenda
Takaku, H.; Nashimoto, M.
Escherichia coli tRNase Z can shut down growth probably by removing amino acids from aminoacyl-tRNAs
Genes Cells
13
1087-1097
2008
Escherichia coli
brenda
Minagawa, A.; Ishii, R.; Takaku, H.; Yokoyama, S.; Nashimoto, M.
The flexible arm of tRNase Z is not essential for pre-tRNA binding but affects cleavage site selection
J. Mol. Biol.
381
289-299
2008
Bacillus subtilis, Escherichia coli, Pyrobaculum aerophilum, Thermoplasma acidophilum, Thermotoga maritima
brenda
Dutta, T.; Deutscher, M.P.
Catalytic properties of RNase BN/RNase Z from Escherichia coli: RNase BN is both an exo- and endoribonuclease
J. Biol. Chem.
284
15425-15431
2009
Escherichia coli
brenda
Hartmann, R.K.; Goessringer, M.; Spaeth, B.; Fischer, S.; Marchfelder, A.
The making of tRNAs and more - RNase P and tRNase Z
Prog. Mol. Biol. Transl. Sci.
85
319-368
2009
Aeropyrum pernix, Archaeoglobus fulgidus, Bacillus subtilis, Borreliella burgdorferi, Chlamydia trachomatis, Clostridium perfringens, Deinococcus radiodurans, Escherichia coli, Halobacterium sp., Haloferax volcanii, Lactococcus lactis, Methanocaldococcus jannaschii, Methanopyrus kandleri, Methanosarcina mazei, Methanothermobacter thermautotrophicus, Nanoarchaeum equitans, Pyrobaculum aerophilum, Pyrococcus abyssi, Pyrococcus furiosus, Saccharolobus solfataricus, Synechocystis sp. PCC 6803, Thermoplasma acidophilum, Thermotoga maritima, Treponema pallidum, Triticum aestivum
brenda
Dutta, T.; Deutscher, M.P.
Mode of action of RNase BN/RNase Z on tRNA precursors: RNase BN does not remove the CCA sequence from tRNA
J. Biol. Chem.
285
22874-22881
2010
Escherichia coli
brenda