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physiological function

-
isoforms TUT7/ZCCHC6, TUT4/ZCCHC11, and TUT2/PAPD4/GLD2 are the terminal uridylyltransferases responsible for pre-miRNA mono-uridylation. The terminal uridylyl transferases act specifically on dsRNAs with a 1 nucleotide 3' overhang, thereby creating a 2 nucleotide 3' overhang. Depletion of terminal uridylyl transferases reduces let-7 microRNA levels and disrupts let-7 function. Although the let-7 suppressor, Lin28, induces inhibitory oligo-uridylation in embryonic stem cells, mono-uridylation occurs in somatic cells lacking Lin28 to promote let-7 biogenesis; isoforms TUT7/ZCCHC6, TUT4/ZCCHC11, and TUT2/PAPD4/GLD2 are the terminal uridylyltransferases responsible for pre-miRNA mono-uridylation. The terminal uridylyl transferases act specifically on dsRNAs with a 1 nucleotide 3' overhang, thereby creating a 2 nucleotide 3' overhang. Depletion of terminal uridylyl transferases reduces let-7 microRNA levels and disrupts let-7 function. Although the let-7 suppressor, Lin28, induces inhibitory oligo-uridylation in embryonic stem cells, mono-uridylation occurs in somatic cells lacking Lin28 to promote let-7 biogenesis
physiological function
-
isoform RET2 is an integral component of the RNA editing core complex RECC. Interaction of RET2 with RECC is accomplished via a protein-protein contact between its middle domain and structural subunit MP81. The recombinant RET2 catalyzes a faithful editing on gapped precleaved double-stranded RNA substrates, and this reaction requires an internal monophosphate group at the 5' end of the mRNA 3' cleavage fragment. RET2 processivity is limited to insertion of three U residues. Incorporation into the RECC voids the internal phosphate requirement and allows filling of longer gaps similar to those observed in vivo. Monomeric and RECC-embedded enzymes display a similar bimodal activity, the distributive insertion of a single uracil is followed by a processive extension limited by the number of guiding nucleotides
physiological function
-
isoform RET1 adds U tails to gRNAs, rRNAs, and selected mRNAs and contributes U residues into A/U heteropolymers. Isoform RET1's terminal uridylyl transferase activity is required for the nucleolytic processing of gRNA, rRNA, and mRNA precursors. The U tailās presence does not affect the stability of gRNAs and rRNAs, while transcript-specific uridylylation triggers 3' to 5' mRNA decay. The minicircle-encoded antisense transcripts, which are stabilized by RET1-catalyzed uridylylation, may direct a nucleolytic cleavage of multicistronic precursors
physiological function
isoform Rsp1 associates with uridylyltransferase Rdn1-RNA-dependent RNA polymerase Rdf1 or Rdn1-Rdf2 subcomplexes, creating Rsp1 complexes RSPCs that are physically separate from RNA-dependent RNA polymerase complexes RDRCs. The uridylyltransferase activity of Rdn1 is greatly reduced in RSPCs compared with RDRCs, suggesting enzyme regulation by the alternative partners. Despite the loss of all known RDRC-generated classes of endogenous sRNAs, RSP1 gene knockout is tolerated in growing cells. A minority class of dicer protein Dcr2-dependent sRNAs persists in cells lacking Rsp1 with increased size heterogeneity
physiological function
-
isoforms Zcchc11 and Zcchc6 redundantly control let-7 biogenesis in embryonic stem cells; isoforms Zcchc11 and Zcchc6 redundantly control let-7 biogenesis in embryonic stem cells
physiological function
isoform Tailor preferentially uridylates mirtron hairpins, thereby impeding the production of non-canonical microRNAs. Mirtron selectivity is explained by primary sequence specificity of Tailor, selecting substrates ending with a 3'-guanosine. In contrast to mirtrons, conserved Drosophila precursor micro-RNAs are significantly depleted in 3'-guanosine, thereby escaping regulatory uridylation. Cytoplasmic Tailor is required for miRNA uridylation and normal fertility in flies
physiological function
-
oligo(A)-tailed mRNAs are uridylated by the cytosolic UTP:RNA uridylyltransferase URT1, and URT1 has no major impact on mRNA degradation rates. In absence of uridylation, oligo(A) tails are trimmed, indicating that uridylation protects oligoadenylated mRNAs from 3'-ribonucleolytic attacks. URT1 mutants display an increase in 3'-truncated transcripts
physiological function
isoform HESO1, which uridylates most unmethylated miRNAs in vivo, and isoform URT1 which exhibits nucleotidyl transferase activity on unmethylated miRNA, prefer substrates with different 3'-end nucleotides in vitro and act cooperatively to tail different forms of the same miRNAs in vivo. Both HESO1 and URT1 exhibit nucleotidyl transferase activity on AGO1-bound miRNAs. Although the enzymes are able to add long tails to AGO1-bound miRNAs, the tailed miRNAs remain associated with AGO1. Tailing of AGO1-bound miRNA165/6 drastically reduces the slicing activity of AGO1-miR165/6; URT1 is the single most predominant nucleotidyl transferase that tails miRNAs. URT1 and isoform HESO1, which uridylates most unmethylated miRNAs in vivo, prefer substrates with different 3'-end nucleotides in vitro and act cooperatively to tail different forms of the same miRNAs in vivo. Both HESO1 and URT1 exhibit nucleotidyl transferase activity on AGO1-bound miRNAs. Although the enzymes are able to add long tails to AGO1-bound miRNAs, the tailed miRNAs remain associated with AGO1. Tailing of AGO1-bound miRNA165/6 drastically reduces the slicing activity of AGO1-miR165/6. Monouridylation of miR171a by URT1 endows the miRNA the ability to trigger the biogenesis of secondary siRNAs
physiological function
-
oligo(A)-tailed mRNAs are uridylated by the cytosolic UTP:RNA uridylyltransferase URT1, and URT1 has no major impact on mRNA degradation rates. In absence of uridylation, oligo(A) tails are trimmed, indicating that uridylation protects oligoadenylated mRNAs from 3'-ribonucleolytic attacks. URT1 mutants display an increase in 3'-truncated transcripts
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + (mRNA)n
diphosphate + (mRNA)n+1
-
i.e. total human mRNA
-
-
?
ATP + 5'(ppp)-UGAGGUAGUAGGUUGUAUAGUU-3'
diphosphate + 5'(ppp)-UGAGGUAGUAGGUUGUAUAGUUA-3'
-
i.e. triphosphorylated human let-7a-5p-3p
-
-
?
ATP + 5'-UGAGGUAGUAGGUUGUAUAGUU-3'
diphosphate + 5'-UGAGGUAGUAGGUUGUAUAGUUA-3'
-
i.e. unphosphorylated human let-7a-0P. Gld2 displays an 83fold preference of ATP over UTP
-
-
?
ATP + RNAn
diphosphate + RNAn+1
CTP + 5'(pp)-UGAGGUAGUAGGUUGUAUAGUU-3'
diphosphate + 5'(pp)-UGAGGUAGUAGGUUGUAUAGUUC-3'
-
i.e. diphosphorylated human let-7a-5p-2p
-
-
?
CTP + RNAn
diphosphate + RNAn+1
GTP + miR-122
diphosphate + ?
-
-
-
-
?
GTP + RNAn
diphosphate + RNAn+1
UTP + 5'(p)-UGAGGUAGUAGGUUGUAUAGUU-3'
diphosphate + 5'(p)-UGAGGUAGUAGGUUGUAUAGUUU-3'
-
i.e. monophosphorylated human let-7a-5p. Gld2 displays an 83fold preference of ATP over UTP
-
-
?
UTP + RNAn
diphosphate + RNAn+1
UTP + RNAn containing a terminal G residue
diphosphate + RNAn+1
-
substrate dsRNA
-
-
?
UTP + RNAn containing a terminal U residue
diphosphate + RNAn+1
additional information
?
-
ATP + RNAn

diphosphate + RNAn+1
-
low activity
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
editosomal enzyme form, no activity
-
-
-
CTP + RNAn

diphosphate + RNAn+1
-
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
editosomal enzyme form, no activity
-
-
-
GTP + RNAn

diphosphate + RNAn+1
-
about 50% of the activity with UTP, prefers Mn2+ as divalent cation
-
-
?
GTP + RNAn
diphosphate + RNAn+1
-
editosomal enzyme form, no activity
-
-
-
UTP + RNAn

diphosphate + RNAn+1
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
small guide RNA, i.e. gRNA
-
?
UTP + RNAn
diphosphate + RNAn+1
-
marked specificity for UTP
-
?
UTP + RNAn
diphosphate + RNAn+1
-
responsible for post-transcriptional RNA editing process of mitochondrial transcripts in kinetoplastid protozoans
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of non-coded poly(U) tail to gRNAs
-
?
UTP + RNAn
diphosphate + RNAn+1
-
enzyme preferentially uridylates mirtron hairpins
-
?
UTP + RNAn
diphosphate + RNAn+1
-
3'-poly(A) of virion RNA
-
?
UTP + RNAn
diphosphate + RNAn+1
-
specifically modifies the 3'-UMP terminal of mammalian U6 small nuclear RNA, i.e. snRNA, structural requirements and specificity, overview
-
?
UTP + RNAn
diphosphate + RNAn+1
-
acts as a host factor to initiate RNA synthesis by poliovirus RNA polymerase in vitro
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
RNA substrate specificity, overview
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
editosomal enzyme form shows preference for a 3' terminal A or G, while the mitochondrial enzyme form does not
-
?
UTP + RNAn
diphosphate + RNAn+1
-
mitochondrial enzyme form adds Us at the 3' and the 5' end of the RNA
-
?
UTP + RNAn
diphosphate + RNAn+1
-
kinetoplast RNA
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
the mitochondrial enzyme adds a single U to the 3'-end of single-stranded RNA
-
?
UTP + RNAn
diphosphate + RNAn+1
-
involved in uridine insertion in the editing process of RNA
-
?
UTP + RNAn
diphosphate + RNAn+1
-
responsible for post-transcriptional RNA editing process of mitochondrial transcripts in kinetoplastid protozoans
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of non-coded poly(U) tail to gRNAs
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of non-coded poly(U) tail to gRNAs
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of primarily single U to single-stranded RNA, addition of the number of Us specified by a guide RNA to insertion editing-like substrates
-
?
UTP + RNAn
diphosphate + RNAn+1
-
TbMP57 TUTase, an enzyme thought to act exclusively in U-insertion, can also function within the U-deletion cycle, after cleavage and 3'-U-exo but before U-deletional cycle
-
-
?
UTP + RNAn
diphosphate + RNAn+1
a template-independent RNA nucleotidyltransferases that specifically recognize UTP, it possesses conserved catalytic and UTP recognition domains. A single nucleoside triphosphate is bound in the active site by a complex network of interactions between amino acid residues, a magnesium ion and highly ordered water molecules with the UTPās base, ribose and phosphate moieties, structure-function analysis, overview
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
invariant arginine residues 144 and 435 positioned in the vicinity of the UTP-binding site are critical for isoform RET2 activity on single-stranded and double-stranded RNAs, as well as function in vivo. Recognition of a double-stranded RNA, which resembles a guide RNA/mRNA duplex, is further facilitated by multipoint contacts across the RET2-specific middle domain
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
TbMP57 TUTase, an enzyme thought to act exclusively in U-insertion, can also function within the U-deletion cycle, after cleavage and 3'-U-exo but before U-deletional cycle
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
the enzyme requires a single-stranded oligoribonucleotide or polyribonucleotide with a free terminal 3'-OH as primer, e.g. oligoA20, tRNAAsp, E. coli RNA, alfalafa mosaic virus RNA 4
-
?
UTP + RNAn
diphosphate + RNAn+1
-
marked specificity for UTP
-
?
UTP + RNAn
diphosphate + RNAn+1
-
RNA substrate specificity, overview
-
?
UTP + RNAn
diphosphate + RNAn+1
-
RNA uridylyltransferase might function in uridylating specific proteins, RNA is not a natural substrate
-
?
UTP + RNAn containing a terminal U residue

diphosphate + RNAn+1
-
-
-
-
?
UTP + RNAn containing a terminal U residue
diphosphate + RNAn+1
-
substrate dsRNA
-
-
?
additional information

?
-
enzyme shows strong preference for uridine and a distributive activity for the first added nucleotides. URT1 uridylates oligoadenylated mRNAs
-
-
-
additional information
?
-
HESO1 exhibits nucleotidyl transferase activity on methylated miRNA in vitro. HESO1 has a clear preference for miR158A-U. miR158A-G is the second most preferred substrate
-
-
-
additional information
?
-
URT1 exhibits nucleotidyl transferase activity on unmethylated miRNA in vitro. URT1 shows a strong preference for miR158 ending in A, miR158A-C, miR158A-G, and miR158A-U are similarly used by URT1
-
-
-
additional information
?
-
enzyme shows strong preference for uridine and a distributive activity for the first added nucleotides. URT1 uridylates oligoadenylated mRNAs
-
-
-
additional information
?
-
-
human Gld2 is a bona fide adenylyltransferase with only weak activity toward other nucleotides. Gld2 is a promiscuous enzyme, with activity toward miRNA, pre-miRNA, and polyadenylated RNA substrates. Gld2 shows a clear preference for ATP in the presence of all four NTPs. Apo-Gld2 activity is restricted to adding single nucleotides and processivity likely relies on additional RNA-binding proteins
-
-
-
additional information
?
-
-
enzyme interacts with a minor fraction of total RNA ligase
-
-
-
additional information
?
-
-
post-transcriptional uridylylation of guide RNAs by RNA editing TUTase 1 or RET1, a multi-functional RNA processing enzyme, and U-insertion mRNA editing by RNA editing TUTase 2 or RET2, biological functions of TUT isozymes, RNA processing in mitochondria of trypanosomes, detailed overview
-
-
-
additional information
?
-
-
UTP recognition mechanism, overview. The NTD-CTD bi-domain catalytic modules shared by TUTases and non-canonical poly(A) polymerases, ncPAPs, are quite promiscuous in NTP binding, NTP selectivity of TUTase-like catalytic modules, RNA specificity, overview
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
reduction of isozyme RET1 leads to decrease in edited RNA and inhibited growth, lowers the uridine insertion and leads predominantly to shorter gRNAs
-
-
-
additional information
?
-
-
down-regulation of isozyme RET2 inhibits growth and in vivo uridine insertion, but has no effect on the length of gRNAs
-
-
-
additional information
?
-
-
many editing changes are developmentally regulated
-
-
-
additional information
?
-
-
down-regulation of RET1, but not of RET2, affects length distribution of gRNA 3' oligo(U) tails
-
-
-
additional information
?
-
-
Inhibition of RNA editing by down-regulation of expression of the mitochondrial RNA editing TUTase 1 by RNA interference has profound effects on kinetoplast biogenesis in Trypanosoma brucei procyclic cells. De novo synthesis of the apocytochrome b and cytochrome oxidase subunit I proteins is no longer detectable after 3 days of RNAi. The effect on protein synthesis correlates with a decline in the levels of the assembled mitochondrial respiratory complexes III and IV, and also with cyanide-sensitive oxygen uptake. The steady-state levels of nuclear-encoded subunits of complexes III and IV are also significantly decreased. Because the levels of the corresponding mRNAs are not affected, the observed effect is likely due to an increased turnover of these imported mitochondrial proteins. This induced protein degradation is selective for components of complexes III and IV, because little effect is observed on components of the F1-F0 -ATPase complex and on several other mitochondrial proteins
-
-
-
additional information
?
-
-
post-transcriptional uridylylation of guide RNAs by RNA editing TUTase 1 or RET1, a multi-functional RNA processing enzyme, and U-insertion mRNA editing by RNA editing TUTase 2 or RET2, biological functions of TUT isozymes, RNA processing in mitochondria of trypanosomes, detailed overview
-
-
-
additional information
?
-
TUT4 substrate specificity toward nucleoside triphosphate substrates with a synthetic 5'-radiolabeled 24-mer RNA as a primer, in presence of Mg2+ ions TUT4 preferentially incorporates uridylyl residues but the reaction with CTP is also detectable, TbTUT4 incorporates only one deoxynucleotide into RNA, overview. UTP binding site structure and structure-activity analysis
-
-
-
additional information
?
-
-
UTP recognition mechanism, overview. UTP specificity is determined primarily by the two closely positioned carboxylic residues, D297/D421 and E300/E424, which coordinate a crucial water molecule indicated in TUT4/RET2, uracil base interactions with invariant amino acids N147, S148, Y189, D297, E300 of TUT4. The NTD-CTD bi-domain catalytic modules shared by TUTases and non-canonical poly(A) polymerases, ncPAPs, are quite promiscuous in NTP binding, NTP selectivity of TUTase-like catalytic modules, RNA specificity, overview
-
-
-
additional information
?
-
-
isoform RET1 adds U tails to gRNAs, rRNAs, and selected mRNAs and contributes U residues into A/U heteropolymers. Isoform RET1's terminal uridylyl transferase activity is required for the nucleolytic processing of gRNA, rRNA, and mRNA precursors. The U tailās presence does not affect the stability of gRNAs and rRNAs, while transcript-specific uridylylation triggers 3' to 5' mRNA decay. The minicircle-encoded antisense transcripts, which are stabilized by RET1-catalyzed uridylylation, may direct a nucleolytic cleavage of multicistronic precursors
-
-
-
additional information
?
-
-
recombinant RET2 catalyzes a faithful editing on gapped precleaved double-stranded RNA substrates, and this reaction requires an internal monophosphate group at the 5' end of the mRNA 3' cleavage fragment. RET2 processivity is limited to insertion of three U residues. Incorporation into the RNA editing core complex RECC allows filling of longer gaps similar to those observed in vivo. Monomeric and RECC-embedded enzymes display a similar bimodal activity, the distributive insertion of a single uracil is followed by a processive extension limited by the number of guiding nucleotides. The distributive +1 insertion creates a substrate for the processive gap-filling reaction. Upon base-pairing of the +1 extended 5' cleavage fragment with a guiding nucleotide, this substrate is recognized by RET2 in a different mode compared to the product of the initial nucleolytic cleavage. Therefore, RET2 distinguishes base pairs in gapped RNA substrates
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UTP + RNAn
diphosphate + RNAn+1
additional information
?
-
UTP + RNAn

diphosphate + RNAn+1
-
responsible for post-transcriptional RNA editing process of mitochondrial transcripts in kinetoplastid protozoans
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of non-coded poly(U) tail to gRNAs
-
?
UTP + RNAn
diphosphate + RNAn+1
-
acts as a host factor to initiate RNA synthesis by poliovirus RNA polymerase in vitro
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
Q381M1
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
involved in uridine insertion in the editing process of RNA
-
?
UTP + RNAn
diphosphate + RNAn+1
-
responsible for post-transcriptional RNA editing process of mitochondrial transcripts in kinetoplastid protozoans
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of non-coded poly(U) tail to gRNAs
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of non-coded poly(U) tail to gRNAs
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of primarily single U to single-stranded RNA, addition of the number of Us specified by a guide RNA to insertion editing-like substrates
-
?
UTP + RNAn
diphosphate + RNAn+1
-
RNA uridylyltransferase might function in uridylating specific proteins, RNA is not a natural substrate
-
?
additional information

?
-
-
enzyme interacts with a minor fraction of total RNA ligase
-
-
-
additional information
?
-
-
post-transcriptional uridylylation of guide RNAs by RNA editing TUTase 1 or RET1, a multi-functional RNA processing enzyme, and U-insertion mRNA editing by RNA editing TUTase 2 or RET2, biological functions of TUT isozymes, RNA processing in mitochondria of trypanosomes, detailed overview
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
reduction of isozyme RET1 leads to decrease in edited RNA and inhibited growth, lowers the uridine insertion and leads predominantly to shorter gRNAs
-
-
-
additional information
?
-
-
down-regulation of isozyme RET2 inhibits growth and in vivo uridine insertion, but has no effect on the length of gRNAs
-
-
-
additional information
?
-
-
many editing changes are developmentally regulated
-
-
-
additional information
?
-
-
down-regulation of RET1, but not of RET2, affects length distribution of gRNA 3' oligo(U) tails
-
-
-
additional information
?
-
-
Inhibition of RNA editing by down-regulation of expression of the mitochondrial RNA editing TUTase 1 by RNA interference has profound effects on kinetoplast biogenesis in Trypanosoma brucei procyclic cells. De novo synthesis of the apocytochrome b and cytochrome oxidase subunit I proteins is no longer detectable after 3 days of RNAi. The effect on protein synthesis correlates with a decline in the levels of the assembled mitochondrial respiratory complexes III and IV, and also with cyanide-sensitive oxygen uptake. The steady-state levels of nuclear-encoded subunits of complexes III and IV are also significantly decreased. Because the levels of the corresponding mRNAs are not affected, the observed effect is likely due to an increased turnover of these imported mitochondrial proteins. This induced protein degradation is selective for components of complexes III and IV, because little effect is observed on components of the F1-F0 -ATPase complex and on several other mitochondrial proteins
-
-
-
additional information
?
-
-
post-transcriptional uridylylation of guide RNAs by RNA editing TUTase 1 or RET1, a multi-functional RNA processing enzyme, and U-insertion mRNA editing by RNA editing TUTase 2 or RET2, biological functions of TUT isozymes, RNA processing in mitochondria of trypanosomes, detailed overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.000228
ATP
-
pH 8.0, 37°C
0.055
CTP
-
pH 8.0, 37°C
0.0126 - 0.0208
RNAn containing a terminal U residue
-
additional information
additional information
steady-state enzyme kinetics, overview
-
0.0002
RNA

; mutant S148A
0.0004
RNAn

-
RNA editing core complex RECC, pH 8.0, temperature not specified in the publication
0.0025
RNAn
-
recombinant enzyme, pH 8.0, temperature not specified in the publication
0.0126
RNAn containing a terminal U residue

-
recombinant enzyme, pH 8.0, temperature not specified in the publication
-
0.0208
RNAn containing a terminal U residue
-
RNA editing core complex RECC, pH 8.0, temperature not specified in the publication
-
0.0004
UTP

mutant R307A
0.0005
UTP
-
mutant V271R/C83F, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.0006
UTP
-
mutant C83F, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.0025
UTP
-
wild-type, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.0026
UTP
-
mutant C83F, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
0.0028
UTP
-
mutant V271R, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.003
UTP
-
mutant V271R/C83F, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
0.0081
UTP
-
mutant K149A, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.0126
UTP
-
wild-type, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
0.0209
UTP
-
mutant V271R, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
0.169
UTP
-
pH 8.0, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0000293
ATP
-
pH 8.0, 37°C
0.000914
CTP
-
pH 8.0, 37°C
0.000403
GTP
-
pH 8.0, 37°C
0.0015 - 0.0033
RNAn containing a terminal U residue
-
0.00166
RNA

mutant S188A
0.0003
RNAn

-
recombinant enzyme, pH 8.0, temperature not specified in the publication
0.0007
RNAn
-
RNA editing core complex RECC, pH 8.0, temperature not specified in the publication
0.0015
RNAn containing a terminal U residue

-
RNA editing core complex RECC, pH 8.0, temperature not specified in the publication
-
0.0033
RNAn containing a terminal U residue
-
recombinant enzyme, pH 8.0, temperature not specified in the publication
-
0.00002
UTP

-
mutant K149A, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.00003
UTP
-
mutant V271R, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.000033
UTP
mutant R121A
0.00005
UTP
-
mutant C83F, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.0000666
UTP
mutant D297N
0.00012
UTP
-
mutant V271R/C83F, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.000133
UTP
mutant R307A
0.000248
UTP
-
pH 8.0, 37°C
0.0003
UTP
-
wild-type, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.0012
UTP
-
mutant V271R, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
0.0015
UTP
-
mutant C83F, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
0.0018
UTP
-
mutant V271R/C83F, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
0.003
UTP
-
wild-type, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.128
ATP
-
pH 8.0, 37°C
0.0166
CTP
-
pH 8.0, 37°C
0.0018
GTP
-
pH 8.0, 37°C
0.067 - 0.267
RNAn containing a terminal U residue
-
0.133
RNAn

-
recombinant enzyme, pH 8.0, temperature not specified in the publication
0.167
RNAn
-
RNA editing core complex RECC, pH 8.0, temperature not specified in the publication
0.067
RNAn containing a terminal U residue

-
RNA editing core complex RECC, pH 8.0, temperature not specified in the publication
-
0.267
RNAn containing a terminal U residue
-
recombinant enzyme, pH 8.0, temperature not specified in the publication
-
0.0015
UTP

-
pH 8.0, 37°C
0.0053
UTP
-
mutant K149A, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.0058
UTP
-
mutant V271R, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
0.0097
UTP
-
mutant V271R, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.0567
UTP
-
mutant C83F, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
0.0867
UTP
-
mutant C83F, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.117
UTP
-
wild-type, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.21
UTP
-
mutant V271R/C83F, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.25
UTP
-
wild-type, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
0.6
UTP
-
mutant V271R/C83F, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
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