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Information on EC 2.7.1.160 - 2'-phosphotransferase
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2.7.1.160 2'-phosphotransferaseIUBMB Comments
Catalyses the final step of tRNA splicing in the yeast Saccharomyces cerevisiae . The reaction takes place in two steps: in the first step, the 2'-phosphate on the RNA substrate is ADP-ribosylated, causing the relase of nicotinamide and the formation of the reaction intermediate, ADP-ribosylated tRNA . In the second step, dephosphorylated (mature) tRNA is formed along with ADP ribose 1''-2''-cyclic phosphate. Highly specific for oligonucleotide substrates bearing an internal 2'-phosphate. Oligonucleotides with only a terminal 5'- or 3'-phosphate are not substrates .
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Word Map
- 2.7.1.160
-
2'-phosphate
- junction
- adp-ribose
-
adp-ribosylation
-
2.7.1.23
- pre-trnas
-
phosphodiester
-
2'-phosphorylated
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
Synonyms
2'-phosphotransferase, ApeTpt1, AtPt, CTHT_0025470, HeLa cell 2'-phosphotransferase, human TRPT1, KptA, kptA1, mTPT1, NAD+-dependent 2'-phosphotransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2'-phosphotransferase
ApeTpt1
CTHT_0025470
KptA
kptA1
mTPT1
NAD-dependent RNA 2'-phosphotransferase
RNA 2'-phosphotransferase
RslTpt1
Tpt1
Tpt1p
tRNA 2'-phosphotransferase
2'-phosphotransferase
-
removes 2'-phosphate from the splice junction of the precursor t-RNA
NAD-dependent RNA 2'-phosphotransferase
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847
-
-
Tpt1p
-
Mammalian genomes encode a single known functional homolog of yeast Tpt1p.
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2'-phospho-[ligated tRNA] + NAD+ = mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho-group transfer
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
2'-phospho-[ligated tRNA]:NAD+ phosphotransferase
Catalyses the final step of tRNA splicing in the yeast Saccharomyces cerevisiae [2]. The reaction takes place in two steps: in the first step, the 2'-phosphate on the RNA substrate is ADP-ribosylated, causing the relase of nicotinamide and the formation of the reaction intermediate, ADP-ribosylated tRNA [6]. In the second step, dephosphorylated (mature) tRNA is formed along with ADP ribose 1''-2''-cyclic phosphate. Highly specific for oligonucleotide substrates bearing an internal 2'-phosphate. Oligonucleotides with only a terminal 5'- or 3'-phosphate are not substrates [1].
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CAS REGISTRY NUMBER
COMMENTARY
126905-00-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
18-mer 2' phosphorylated RNA + NAD+
?
-
ACAAGACUGUAA-(2Ć¢ĀĀ-phosphate)AUCUUG
-
-
?
2'-phospho-(ligated tRNA) + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide + H+
-
-
-
-
?
2'-phospho-(ligated tRNA) + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide + H2O
yeasts
-
enzyme catalyzes final step in tRNA splicing
-
-
?
2'-phospho-(ligated tRNA) + NAD+
mature tRNA + ADP-ribose1'',2''-phosphate + nicotinamide + H2O
-
last step in the pre-tRNA splicing process
-
-
ir
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
3-mer 2' phosphorylated RNA + NAD+
?
-
AU-(2Ć¢ĀĀ-phosphate)U
-
-
?
8-mer 2' phosphorylated RNA + NAD+
?
-
GUAA-(2Ć¢ĀĀ-phosphate)AUCU
-
-
?
NAD+ + trinucleotide substrate
ADP-ribosylated RNA
-
requires ca. 0.0004 mM Tpt1 K69A/R71S, only 0.0000003 mM Tpt1p is required for similar or greater product formation
-
-
?
18-mer 2' phosphorylated RNA
?
-
pACAAGACUCUAA-(2Ć¢ĀĀ-phosphate)AUCUUG
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
production of a reaction intermediate, nicotinamide release occurs during intermediate formation, KptA can catalyze the conversion of the intermediate to both product and the original substrate
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
minimal substrate is a dinucleotide containing an internal 2' phosphate, 600fold more specific for 2'phosphates than for eihter 5'- or 3'-terminal phosphates, 20fold more specific for internal 2' phosphates than for terminal 2' 3', or 2'3'-cyclic phosphates, at least 50fold more specific for internal 2' phosphates than terminal 2' phosphates
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
mTpt1 can catalyze the conversion of the KptA-generated intermediate to both product and the original substrate
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
minimal substrate is a dinucleotide containing an internal 2'-phosphate
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
specifity for substrates bearing an internal 2'-phosphate
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
Tpt1 can catalyze the conversion of the KptA-generated intermediate to both product and the original substrate
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
tRNA_Leu_UAG, tRNA_SER, tRNA_LEU_CAA, tRNA_TYR, tRNA_LYS, tRNA_PRO1, tRNA_PRO2, tRNA_PHE, unidentified tRNA
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
98% conversion by ApeTpt1
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Aeropyrum pernix ATCC 700893
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Aeropyrum pernix ATCC 700893
98% conversion by ApeTpt1
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
98% conversion by ApeTpt1
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Aeropyrum pernix JCM 9820
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Aeropyrum pernix JCM 9820
98% conversion by ApeTpt1
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Aeropyrum pernix NBRC 100138
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Aeropyrum pernix NBRC 100138
98% conversion by ApeTpt1
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Agrobacterium tumefaciens C58 / ATCC 33970
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
13% conversion by the Archaeoglobus fulgidus enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
13% conversion by the Archaeoglobus fulgidus enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
13% conversion by the Archaeoglobus fulgidus enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
13% conversion by the Archaeoglobus fulgidus enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
13% conversion by the Archaeoglobus fulgidus enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
21% conversion by the Chaetomium thermophilum enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
21% conversion by the Chaetomium thermophilum enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
21% conversion by the Chaetomium thermophilum enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
21% conversion by the Chaetomium thermophilum enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
20% conversion by the Pyrococcus horikoshii enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
20% conversion by the Pyrococcus horikoshii enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
20% conversion by the Pyrococcus horikoshii enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
20% conversion by the Pyrococcus horikoshii enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
20% conversion by the Pyrococcus horikoshii enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
20% conversion by the Pyrococcus horikoshii enzyme
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Runella slithyformis ATCC 49304
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
3-mer 2' phosphorylated RNA
?
-
pApa-(2Ć¢ĀĀ-phosphate)pA, pUpU-(2Ć¢ĀĀ-phosphate)pU, pAAA-(2Ć¢ĀĀ-phosphate)p and pAAA-(2Ć¢ĀĀ-phosphate)pOCH3
-
-
?
3-mer 2' phosphorylated RNA
?
-
pApA-(2Ć¢ĀĀ-phosphate)pA, pApU-(2Ć¢ĀĀ-phosphate)pA, pUpU-(2Ć¢ĀĀ-phosphate)pU, pApApA-(2Ć¢ĀĀ-phosphate),pApApA-(2Ć¢ĀĀ-phosphate)p, pApApA-(2Ć¢ĀĀ-phosphate)1OCH3
-
-
?
additional information
?
-
enzyme ApeTpt1 catalyzes a one-step synthesis of a 5'-phospho-ADP-ribosylated cap structure (with no subsequent 5'-phosphotransferase step). ApeTpt1 caps RNA or DNA 5'-phosphate ends with ADP-ribose. pDNA and pRNA substrates are capped quantitatively at saturating enzyme in preence of NAD+. ApeTpt1 with 200 nM 10mer 5' 32P-labeled RNA or DNA oligonucleotides of identical nucleotide sequence (excepting T for U in DNA versus RNA) in the presence of 1 mM NAD+ resulted in the conversion of the substrates into RNA and DNA products of slower electrophoretic mobility. The 32P-labeled capped oligonucleotides are gel-purified and reacted with ApeTpt1 in the presence of 1 mM nicotinamide. This results in decapping of 20% of the ADPR-pDNA substrate to regenerate the pDNA strand
-
-
-
additional information
?
-
-
enzyme ApeTpt1 catalyzes a one-step synthesis of a 5'-phospho-ADP-ribosylated cap structure (with no subsequent 5'-phosphotransferase step). ApeTpt1 caps RNA or DNA 5'-phosphate ends with ADP-ribose. pDNA and pRNA substrates are capped quantitatively at saturating enzyme in preence of NAD+. ApeTpt1 with 200 nM 10mer 5' 32P-labeled RNA or DNA oligonucleotides of identical nucleotide sequence (excepting T for U in DNA versus RNA) in the presence of 1 mM NAD+ resulted in the conversion of the substrates into RNA and DNA products of slower electrophoretic mobility. The 32P-labeled capped oligonucleotides are gel-purified and reacted with ApeTpt1 in the presence of 1 mM nicotinamide. This results in decapping of 20% of the ADPR-pDNA substrate to regenerate the pDNA strand
-
-
-
additional information
?
-
Aeropyrum pernix ATCC 700893
enzyme ApeTpt1 catalyzes a one-step synthesis of a 5'-phospho-ADP-ribosylated cap structure (with no subsequent 5'-phosphotransferase step). ApeTpt1 caps RNA or DNA 5'-phosphate ends with ADP-ribose. pDNA and pRNA substrates are capped quantitatively at saturating enzyme in preence of NAD+. ApeTpt1 with 200 nM 10mer 5' 32P-labeled RNA or DNA oligonucleotides of identical nucleotide sequence (excepting T for U in DNA versus RNA) in the presence of 1 mM NAD+ resulted in the conversion of the substrates into RNA and DNA products of slower electrophoretic mobility. The 32P-labeled capped oligonucleotides are gel-purified and reacted with ApeTpt1 in the presence of 1 mM nicotinamide. This results in decapping of 20% of the ADPR-pDNA substrate to regenerate the pDNA strand
-
-
-
additional information
?
-
enzyme ApeTpt1 catalyzes a one-step synthesis of a 5'-phospho-ADP-ribosylated cap structure (with no subsequent 5'-phosphotransferase step). ApeTpt1 caps RNA or DNA 5'-phosphate ends with ADP-ribose. pDNA and pRNA substrates are capped quantitatively at saturating enzyme in preence of NAD+. ApeTpt1 with 200 nM 10mer 5' 32P-labeled RNA or DNA oligonucleotides of identical nucleotide sequence (excepting T for U in DNA versus RNA) in the presence of 1 mM NAD+ resulted in the conversion of the substrates into RNA and DNA products of slower electrophoretic mobility. The 32P-labeled capped oligonucleotides are gel-purified and reacted with ApeTpt1 in the presence of 1 mM nicotinamide. This results in decapping of 20% of the ADPR-pDNA substrate to regenerate the pDNA strand
-
-
-
additional information
?
-
Aeropyrum pernix JCM 9820
enzyme ApeTpt1 catalyzes a one-step synthesis of a 5'-phospho-ADP-ribosylated cap structure (with no subsequent 5'-phosphotransferase step). ApeTpt1 caps RNA or DNA 5'-phosphate ends with ADP-ribose. pDNA and pRNA substrates are capped quantitatively at saturating enzyme in preence of NAD+. ApeTpt1 with 200 nM 10mer 5' 32P-labeled RNA or DNA oligonucleotides of identical nucleotide sequence (excepting T for U in DNA versus RNA) in the presence of 1 mM NAD+ resulted in the conversion of the substrates into RNA and DNA products of slower electrophoretic mobility. The 32P-labeled capped oligonucleotides are gel-purified and reacted with ApeTpt1 in the presence of 1 mM nicotinamide. This results in decapping of 20% of the ADPR-pDNA substrate to regenerate the pDNA strand
-
-
-
additional information
?
-
Aeropyrum pernix NBRC 100138
enzyme ApeTpt1 catalyzes a one-step synthesis of a 5'-phospho-ADP-ribosylated cap structure (with no subsequent 5'-phosphotransferase step). ApeTpt1 caps RNA or DNA 5'-phosphate ends with ADP-ribose. pDNA and pRNA substrates are capped quantitatively at saturating enzyme in preence of NAD+. ApeTpt1 with 200 nM 10mer 5' 32P-labeled RNA or DNA oligonucleotides of identical nucleotide sequence (excepting T for U in DNA versus RNA) in the presence of 1 mM NAD+ resulted in the conversion of the substrates into RNA and DNA products of slower electrophoretic mobility. The 32P-labeled capped oligonucleotides are gel-purified and reacted with ApeTpt1 in the presence of 1 mM nicotinamide. This results in decapping of 20% of the ADPR-pDNA substrate to regenerate the pDNA strand
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide, and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide, and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide, and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide, and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide, and (ii)transesterification of the ADP-ribose O2''- to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide; and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances
-
-
-
additional information
?
-
-
Comparison of incorporation of 3H-tyrosine and 35S-methionine/cysteine into total proteins confirms that wild-type and Trpt1-/-cells have similar incorporation rates of either amino acid.
-
-
?
additional information
?
-
-
the enzyme Tpt1 removes an internal RNA 2'-phosphate via a two-step reaction in which: (i) the 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and nicotinamide, and (ii)transesterification of the ADP-ribose O2'' to the RNA 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate. Because step 2 is much faster than step 1, the ADP-ribosylated RNA intermediate is virtually undetectable under normal circumstances. Runella Tpt1 (RslTpt1) efficiently removes an internal 2'-phosphate from a DNA substrate. RslTpt1 removes the 2'-phosphate from the 2'-fluoroarabinonucleic acid (2'-FANA) substrate, albeit with about 7fold lower specific activity compared to the 6mer 2'-phosphate RNA control substrate. The 2'-phospho-ADP-ribosylated intermediate accumulates to an extent of 4% of total labeled RNA at low enzyme concentrations. Phosphorothioate (PS) modifications of the 3'-5'-phosphodiester backbone of DNA and 2'-FANA oligonucleotides (PS-DNA and PS-2'-FANA oligos) give substrates that are completely converted to 2'-hydroxy products by RslTpt1 but with reduced activity
-
-
-
additional information
?
-
yeasts
-
synthesis of 5'-Lv-2'-DMT-3'-phosphoramidite-G monomer containing an internal 2-phosphate for incorporation in synthetic RNA in order to construct a fluorescent oligoribonucleotide probe for a high throughput screening assay against yeast Tpt1p.
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2'-phospho-(ligated tRNA) + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide + H+
-
-
-
-
?
2'-phospho-(ligated tRNA) + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide + H2O
yeasts
-
enzyme catalyzes final step in tRNA splicing
-
-
?
2'-phospho-(ligated tRNA) + NAD+
mature tRNA + ADP-ribose1'',2''-phosphate + nicotinamide + H2O
-
last step in the pre-tRNA splicing process
-
-
ir
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
additional information
?
-
-
Comparison of incorporation of 3H-tyrosine and 35S-methionine/cysteine into total proteins confirms that wild-type and Trpt1-/-cells have similar incorporation rates of either amino acid.
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Aeropyrum pernix ATCC 700893
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Aeropyrum pernix JCM 9820
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Aeropyrum pernix NBRC 100138
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Agrobacterium tumefaciens C58 / ATCC 33970
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
Runella slithyformis ATCC 49304
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
UMP, SAMP, cAMP, UTP, CTP, GTP, ATP and derivatives of NAD+ like NMN, ADP-ribose, ATP-ribose, NADPH, NADP+, NADH do not support dephosphorylation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ApGpApUpUpUpApC
-
oligonucleotide, which lacks secondary structure and has no terminal phosphate
PS-2'-FANA oligonucleotides
-
phosphorothioate (PS) modifications of the 3'-5' phosphodiester backbone of DNA and 2'-FANA oligonucleotides (PS-DNA and PS-2'-FANA oligos) give substrates that are completely converted to 2'-hydroxy products by RslTpt1. Runella Tpt1 specific activity is reduced by 11fold and 7fold, respectively, by the PS modifications of DNA and 2'-FANA substrates
-
PS-DNA oligonucleotides
-
phosphorothioate (PS) modifications of the 3'-5'-phosphodiester backbone of DNA and 2'-FANA oligonucleotides (PS-DNA and PS-2'-FANA oligos) give substrates that are completely converted to 2'-hydroxy products by RslTpt1. Runella Tpt1 specific activity is reduced by 11fold and 7fold, respectively, by the PS modifications of DNA and 2'-FANA substrates
-
[pre-tRNA]
-
intron-containing yeast [pre-tRNA], which has the same structure as mature yeast [tRNA], except in the region of the intron
-
[tRNA]
-
mature Escherichia coli [tRNA], has canonical tRNA structue
-
2'-fluoroarabinose
replacing the NMN ribose of NAD+ with 2'-fluoroarabinose (thereby eliminating the ribose O2''-nucleophile) results in durable trapping of RNA-2'-phospho-ADP-fluoroarabinose as a dead-end product of step 1. Low to moderate utilization of ara-2''F-NAD+ as a substrate by Chaetomium thermophilum Tpt1 results in partial trapping of the step 1 reaction product
-
2'-fluoroarabinose
replacing the NMN ribose of NAD+ with 2'-fluoroarabinose (thereby eliminating the ribose O2'' nucleophile) results in durable trapping of RNA-2'-phospho-ADP-fluoroarabinose as a dead-end product of step 1. High utilization of ara-2''F-NAD+ as a substrate by Clostridium thermocellum Tpt1 does indeed results in trapping of the step 1 reaction product
-
2'-fluoroarabinose
-
replacing the NMN ribose of NAD+ with 2'-fluoroarabinose (thereby eliminating the ribose O2'' nucleophile) results in durable trapping of RNA-2'-phospho-ADP-fluoroarabinose as a dead-end product of step 1. High utilization of ara-2''F-NAD+ as a substrate by Runella slithyformis Tpt1 does indeed results in trapping of the step 1 reaction product
-
ara-2''F-NAD+
Chaetomium Tpt1 forms the dead-end product in the presence of 0.05 mM ara-2''F-NAD+, though the extent of substrate conversion is low
-
ara-2''F-NAD+
human Tpt1 effects no detectable reaction of the 2'-phosphate RNA substrate in the presence of 0.05 mM ara-2''F-NAD+
-
arabinose-2'-phosphate
replacement of the RNA ribose-2'-phosphate nucleotide with arabinose-2'-phosphate selectively slows step 2 of the reaction pathway and results in the transient accumulation of high levels of the reaction intermediate
-
arabinose-2'-phosphate
replacement of the RNA ribose-2'-phosphate nucleotide with arabinose-2'-phosphate selectively slows step 2 of the reaction pathway and results in the transient accumulation of high levels of the reaction intermediate
-
arabinose-2'-phosphate
-
replacement of the RNA ribose-2'-phosphate nucleotide with arabinose-2'-phosphate selectively slows step 2 of the reaction pathway and results in the transient accumulation of high levels of the reaction intermediate
-
additional information
analysis of chemically modified nucleic acid substrates for activity with bacterial Tpt1 enzymes
-
additional information
analysis of chemically modified nucleic acid substrates for activity with bacterial Tpt1 enzymes, reveals that replacement of the RNA ribose-2'-phosphate nucleotide with arabinose-2'-phosphate selectively slows step 2 of the reaction pathway and results in the transient accumulation of high levels of the reaction intermediate. Replacing the NMN ribose of NAD+ with 2'-fluoroarabinose (thereby eliminating the ribose O2''-nucleophile) results in durable trapping of RNA-2'-phospho-ADP-fluoroarabinose as a dead-end product of step 1. Replacing the NMN ribose of NAD+ with 2'-fluoroarabinose (thereby eliminating the ribose O2''-nucleophile) can result in durable trapping of RNA-2'-phospho-ADP-fluoroarabinose as a dead-end product of step 1. But no utilization of ara-2''F-NAD+ or arabinose-2'-phosphate as substrates by human Tpt1 is detected
-
additional information
analysis of chemically modified nucleic acid substrates for activity with bacterial Tpt1 enzymes
-
additional information
-
analysis of chemically modified nucleic acid substrates for activity with bacterial Tpt1 enzymes
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000017
18-mer 2' phosphorylated RNA
-
pACAAGACUCUAA-(2Ć¢ĀĀ-phosphate)AUCUUG, 30ĆĀ°C
-
0.00015
3-mer 2' phosphorylated RNA
-
pApA-(2Ć¢ĀĀ-phosphate)pA, 30ĆĀ°C
-
0.000325
3-mer 2' phosphorylated RNA
-
pUpU-(2Ć¢ĀĀ-phosphate)pUs, 30ĆĀ°C
-
0.00048
3-mer 2' phosphorylated RNA
-
pApU-(2Ć¢ĀĀ-phosphate)pA, 30ĆĀ°C
-
0.00065
3-mer 2' phosphorylated RNA
-
pApApA-(2Ć¢ĀĀ-phosphate)p, 30ĆĀ°C
-
0.003
3-mer 2' phosphorylated RNA
-
pApApA-(2Ć¢ĀĀ-phosphate)pOCH3, 30ĆĀ°C
-
0.0038
3-mer 2' phosphorylated RNA
-
pAAA-(2Ć¢ĀĀ-phosphate)pOCH3, 37ĆĀ°C
-
0.04
3-mer 2' phosphorylated RNA
-
pApApA-(2Ć¢ĀĀ-phosphate), 30ĆĀ°C
-
0.00002
8-mer 2' phosphorylated RNA
-
pGUAA-(2Ć¢ĀĀ-phosphate)AUCU, 30ĆĀ°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
18-mer 2' phosphorylated RNA
-
pACAAGACUCUAA-(2Ć¢ĀĀ-phosphate)AUCUUG, 30ĆĀ°C
-
0.317
8-mer 2' phosphorylated RNA
-
pGUAA-(2Ć¢ĀĀ-phosphate)AUCU, 30ĆĀ°C
-
0.0057
3-mer 2' phosphorylated RNA
-
pApApA-(2Ć¢ĀĀ-phosphate), 30ĆĀ°C
-
0.147
3-mer 2' phosphorylated RNA
-
pUpU-(2Ć¢ĀĀ-phosphate)pU, 30ĆĀ°C
-
0.15
3-mer 2' phosphorylated RNA
-
pApApA-(2Ć¢ĀĀ-phosphate)p, 30ĆĀ°C
-
0.45
3-mer 2' phosphorylated RNA
-
pApU-(2Ć¢ĀĀ-phosphate)pA, 30ĆĀ°C
-
0.73
3-mer 2' phosphorylated RNA
-
pApA-(2Ć¢ĀĀ-phosphate)pA, 30ĆĀ°C
-
1.173
3-mer 2' phosphorylated RNA
-
pApApA-(2Ć¢ĀĀ-phosphate)pOCH3, 30ĆĀ°C
-
6.08
3-mer 2' phosphorylated RNA
-
pApApA-(2Ć¢ĀĀ-phosphate)pOCH3, 30ĆĀ°C
-
additional information
18-mer 2' phosphorylated RNA
-
37ĆĀ°C, vmax = 99 fmol/min/ng
-
additional information
3-mer 2' phosphorylated RNA
-
pAAA-(2Ć¢ĀĀ-phosphate)p, 37ĆĀ°C, vmax = 1.4 fmol/min/ng
-
additional information
3-mer 2' phosphorylated RNA
-
pAAA-(2Ć¢ĀĀ-phosphate)pOCH3, 37ĆĀ°C, vmax = 45 fmol/min/ng
-
additional information
3-mer 2' phosphorylated RNA
-
pApA-(2Ć¢ĀĀ-phosphate)pA, 37ĆĀ°C, vmax = 280 fmol/min/ng
-
additional information
3-mer 2' phosphorylated RNA
-
pUpU-(2Ć¢ĀĀ-phosphate)pU, 37ĆĀ°C, vmax = 1030 fmol/min/ng
-
additional information
8-mer 2' phosphorylated RNA
-
37ĆĀ°C, vmax = 170 fmol/min/ng
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
Despite lack of detectable in vitro RNA 2'-phosphotransferase activity in lysates of cells derived from the Trpt1 knockout mice, there is no evidence for a defect in the unfolded protein response or in tRNA function.
additional information
-
Immunoprecipitation of Trpt1 from heart lysates, followed by immunoblot with an antiserum raised to bacterially expressed murine Trpt1 reveals that Trpt1-/-mice lack 2'-phosphotransferase activity yet retain the ability to translate spliced transcription factor XBP-1 mRNA and synthesize tyrosine-containing proteins at wild-type levels. Heterozygotes express 50% of wild-type levels. Extracts of Trpt1+/+cells have measurable NAD+-dependent 2'-phosphotransferase activity.
additional information
-
200000000 units/mg for recombinant Tpt1 produced in Escherichia coli and 140000000 units/mg for Tpt1 purified from yeast
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18 - 30
-
F27A, R71Q, TPT1(1-220) and TPT1(1-210) cells failed to grow at 37ĆĀ°C on yeast medium/peptone/dextrose agar, R71Q and TPT1(1-210) strains grew slower than wild-type TPT1
18 - 37
-
growth of mutants K16A, K69A, H90A, S91A, H117A, T119A, H142A, R158A and R138K on yeast medium/peptone/dextrose agar, colony sizes were similar to that of wild-type TPT1 cells
25 - 30
-
growth of mutants K16A, Y38A, K69A, F72A, H90A, S91A, H117A, T119A, H142A, R158A, TPT1(1-220) and TPT1(1-210) on 5-fluoroorotic acid agar medium
37 - 95
ApeTpt1 caps the pDNA substrate with high yield (94-100%) at temperatures ranging from 37ĆĀ°C to 65ĆĀ°C and with progressively lower yields at 75ĆĀ°C (68%), 85ĆĀ°C (32%), and 95ĆĀ°C (21%)
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Clostridium thermocellum
UniProt
brenda
Clostridium thermocellum
UniProt
brenda
Clostridium thermocellum
UniProt
brenda
Clostridium thermocellum
UniProt
brenda
Clostridium thermocellum
UniProt
brenda
Clostridium thermocellum
UniProt
brenda
Clostridium thermocellum
UniProt
brenda
plant splicing enzymes fused to GFP by their transient expression in Allium epidermal and Vicia guard cells.
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
Clones from two individually selected heterozygous ES cell lines are injected into blastocysts and the resultant founder chimeras bred to obtain two lines of knockout Trpt1+/- and knockout Trpt1-/-mice.
brenda
-
Upper epidermis of Allium cepa is used for transient expression
brenda
-
Lower leaf epidermis from Vicia faba is used for transient expression
brenda
-
Trpt1+/+ and Trpt1-/-cell lines are obtained by serial passage of SV40-T-antigen transfected mouse embryonic fibroblasts
brenda
additional information
additional information
-
nothing detectable in spleen, small intestine, lung, peripheral blood leukocytes, brain and colon
brenda
additional information
nothing detectable in spleen, small intestine, lung, peripheral blood leukocytes, brain and colon
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme contains chloroplast transit signals at the N-terminus, 2'-phosphotransferase are not required for classical tRNA splicing in chloroplast, it has an alternative function
brenda
-
2'-phosphotransferase shows a tendency to associate with mitochondria
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
RNA repair enzymes catalyze rejoining of an RNA molecule after cleavage of phosphodiester linkages. RNA repair in budding yeast is catalyzed by two separate enzymes that process tRNA exons during their splicing and HAC1 mRNA exons during activation of the unfolded protein response (UPR). The RNA ligase Trl1 (EC 6.5.1.3) joins 2',3'-cyclic phosphate and 5'-hydroxyl RNA fragments, creating a phosphodiester linkage with a 2'-phosphate at the junction. The 2'-phosphate is removed by the 2'-phosphotransferase Tpt1 (EC 2.7.1.160)
physiological function
additional information
evolution
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
evolution
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
evolution
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
evolution
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
evolution
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
evolution
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
evolution
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
evolution
Aeropyrum pernix ATCC 700893
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
Aeropyrum pernix JCM 9820
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
Aeropyrum pernix NBRC 100138
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
evolution
-
wide distribution of Tpt1 enzymes in taxa that have no fungal-type RNA ligase. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-PO4 to a 2'-OH (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
-
malfunction
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
malfunction
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
malfunction
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
malfunction
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
malfunction
the essential functions of TRL1 and TPT1 in budding yeast are bypassed by expressing prespliced, intronless versions of the 10 normally intron-containing tRNAs, indicating this repair pathway does not have additional essential functions. Expression of intronless tRNAs fails to rescue the growth of cells with deletions in components of the SEN complex, implying an additional essential role for the splicing endonuclease. The trl1DELTA and tpt1DELTA mutants accumulate tRNA and HAC1 splicing intermediates indicative of RNA repair defects and are hypersensitive to drugs that inhibit translation. RNA repair mutants have defects in translation. tpt1DELTA mutants grow in the presence of tunicamycin despite reduced accumulation of spliced HAC1 mRNA, while failure to induce the unfolded protein response occurs in trl1DELTA cells grown with tunicamycin is lethal owing to their inability to ligate HAC1 after its cleavage by Ire1. Rescued trl1DELTA and tpt1DELTA cells, RNA repair mutants, have unique phenotypes for both tRNA splicing and HAC1 mRNA splicing during the unfolded protein response. The temperature sensitivity of RNA repair mutants at 37ĆĀ°C is not a consequence of tRNA decay pathway (RTD)
malfunction
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
malfunction
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
malfunction
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
malfunction
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
malfunction
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
malfunction
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
malfunction
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
malfunction
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
malfunction
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
malfunction
-
inhibition of transfer of ADP-ribose from NAD+ to 2'-phosphate RNA results in the accumulation of spliced tRNAs that retain the 2'-phosphate in the anticodon loop, while inhibition of the transesterification step and trapping of the ADP-ribosylated RNA intermediate generates tRNAs with bulky lesions in the anticodon loop
-
physiological function
in bacteria NAD-dependent RNA 2'-phosphotransferase KptA might be an RNA processing enzyme able to repair the RNA damaged by toxic endoribonucleases
physiological function
-
in yeast the NAD-dependent RNA 2'-phosphotransferase KptA is known to participate in tRNA splicing by removing the splice junction 2'-phosphate from ligated tRNA
physiological function
the genomic organization of gene kptA suggests that KptA activity is strictly coordinated with the recycling to NAD of its reaction products
physiological function
-
enzyme Tpt1 catalyzes the transfer of an internal 2'-phosphate moiety (2'-PO4) from a branched 2'-phosphate RNA splice junction to NAD+ to form a clean 2'-hydroxy, 3'-5'-phosphodiester junction, ADP-ribose 1''-2'' cyclic phosphate, and nicotinamide. Recombinant expression of RslTpt1 in a yeast mutant complements a lethal tpt1DELTA knockout phenotype
physiological function
enzyme TPT1 is essential only in the context of the generation of 2'-phosphorylated tRNAs by Trl1
physiological function
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5' phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
physiological function
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
physiological function
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
physiological function
-
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
physiological function
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
physiological function
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
physiological function
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
physiological function
the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
physiological function
-
tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
physiological function
tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
physiological function
tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2''- to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
physiological function
tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate; and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
physiological function
Aeropyrum pernix ATCC 700893
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5' phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5' phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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physiological function
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tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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physiological function
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tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
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physiological function
Aeropyrum pernix JCM 9820
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5' phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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physiological function
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tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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physiological function
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tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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physiological function
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tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2''- to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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physiological function
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tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
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physiological function
Runella slithyformis ATCC 49304
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enzyme Tpt1 catalyzes the transfer of an internal 2'-phosphate moiety (2'-PO4) from a branched 2'-phosphate RNA splice junction to NAD+ to form a clean 2'-hydroxy, 3'-5'-phosphodiester junction, ADP-ribose 1''-2'' cyclic phosphate, and nicotinamide. Recombinant expression of RslTpt1 in a yeast mutant complements a lethal tpt1DELTA knockout phenotype
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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physiological function
Aeropyrum pernix NBRC 100138
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5' phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus. Aeropyrum pernix Tpt1 (ApeTpt1) is particularly adept in this respect
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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physiological function
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tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2''- to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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physiological function
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tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2''- to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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physiological function
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tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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physiological function
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tRNA 2'-phosphotransferase (Tpt1) is an essential enzyme in the fungal and plant tRNA splicing pathways that removes the 2'-phosphate at the splice junction generated by fungal and plant tRNA ligases. Tpt1 catalyzes a two-step reaction whereby: (i) the internal RNA 2'-phosphate attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate, and (ii) transesterification of the ribose O2'' to the 2'-phosphodiester yields 2'-hydroxy RNA and ADP-ribose-1'',2''-cyclic phosphate
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physiological function
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the RNA 2'-phosphotransferase Tpt1 converts an internal RNA 2'-phosphate to a 2'-OH via a two-step NAD+-dependent mechanism in which: (i) the 2'-phosphate attacks the C1'' of NAD+ to expel nicotinamide and form a 2'-phospho-ADP-ribosylated RNA intermediate, and (ii) the ADP-ribose O2'' attacks the phosphate of the RNA 2'-phospho-ADPR intermediate to expel the RNA 2'-OH and generate ADP-ribose 1''-2'' cyclic phosphate. Tpt1 is an essential component of the fungal tRNA splicing pathway that generates a unique 2'-phosphate, 3'-5'-phosphodiester splice junction during tRNA ligation. Tpt1 can catalyze reactions other than RNA 2'-phosphate removal. Whereas all of the Tpt1 enzymes are capable of NAD+-dependent conversion of an internal RNA 2'-phosphate to a 2'-hydroxy (the canonical Tpt1 reaction), a subset of Tpt1 enzymes also catalyze NAD+-dependent ADP-ribosylation of an RNA or DNA 5'-phosphate terminus
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additional information
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologs catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2'- or 3'-terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction
additional information
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction
additional information
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Analysis of the crystal structure of Clostridium thermocellum Tpt1 in a product-mimetic complex with ADP-ribose-1''-phosphate in the NAD+ site and pAp in the RNA site for explaining substrate recognition and transesterification mechanism
additional information
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Runella slithyformis Tpt1 has a Arg-His-Arg-Arg catalytic tetrad in the active site
additional information
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Analysis of the crystal structure of Clostridium thermocellum Tpt1 in a product-mimetic complex with ADP-ribose-1''-phosphate in the NAD+ site and pAp in the RNA site for explaining substrate recognition and transesterification mechanism
-
additional information
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Analysis of the crystal structure of Clostridium thermocellum Tpt1 in a product-mimetic complex with ADP-ribose-1''-phosphate in the NAD+ site and pAp in the RNA site for explaining substrate recognition and transesterification mechanism
-
additional information
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Analysis of the crystal structure of Clostridium thermocellum Tpt1 in a product-mimetic complex with ADP-ribose-1''-phosphate in the NAD+ site and pAp in the RNA site for explaining substrate recognition and transesterification mechanism
-
additional information
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Analysis of the crystal structure of Clostridium thermocellum Tpt1 in a product-mimetic complex with ADP-ribose-1''-phosphate in the NAD+ site and pAp in the RNA site for explaining substrate recognition and transesterification mechanism
-
additional information
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction
-
additional information
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Analysis of the crystal structure of Clostridium thermocellum Tpt1 in a product-mimetic complex with ADP-ribose-1''-phosphate in the NAD+ site and pAp in the RNA site for explaining substrate recognition and transesterification mechanism
-
additional information
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction
-
additional information
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction
-
additional information
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Analysis of the crystal structure of Clostridium thermocellum Tpt1 in a product-mimetic complex with ADP-ribose-1''-phosphate in the NAD+ site and pAp in the RNA site for explaining substrate recognition and transesterification mechanism
-
additional information
-
Tpt1 enzymes from diverse taxa differ in their capacity to use ara-2''F-NAD+ as a substrate. Some Tpt1 orthologues catalyze additional NAD+-dependent ADP-ribosyltransferase reactions, such as ADP-ribose capping of RNA and DNA 5'-phosphate ends and removal of nucleic acid 2' or 3' terminal monophosphates, albeit less vigorously than the canonical internal RNA 2'-phosphate removal reaction. Analysis of the crystal structure of Clostridium thermocellum Tpt1 in a product-mimetic complex with ADP-ribose-1''-phosphate in the NAD+ site and pAp in the RNA site for explaining substrate recognition and transesterification mechanism
-
Show AA Sequence and Transmembrane Helices (2273 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27800
estimated theorethical molecular mass of the deduced translation product
30000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor-diffusion method, multiwavelength anomalous diffraction method at 2.8 angstrom, structure of enzyme of two globular domains, N and C-domains, which form a cleft in the center
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R16A/H17A/R64A/R119A
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site-directed mutagenesis, the R16A, H17A, R64A, and R119A mutations are deemed lethal in vivo
R16A/H17A/R64A/R119A
Runella slithyformis ATCC 49304
-
site-directed mutagenesis, the R16A, H17A, R64A, and R119A mutations are deemed lethal in vivo
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H117A
H142A
H90A
K16A
-
colony size indistinguishable from that of wild-type TPT1 strain
K69A
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colony size indistinguishable from that of wild-type TPT1 strain
K69A/R71S
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this mutant produces a substantial amount of the reaction intermediate
R138A
R138K
-
colony size indistinguishable from that of wild-type TPT1 strain
R158A
-
colony size indistinguishable from that of wild-type TPT1 strain
S91A
T119A
-
colony size indistinguishable from that of wild-type TPT1 strain
Y38A
-
colony size indistinguishable from that of wild-type TPT1 strain
additional information
generation and analysis of diverse mutant strains derived from Saccharomyces cerevisiae strain W303. The essential functions of TRL1 and TPT1 in budding yeast are bypassed by expressing prespliced, intronless versions of the 10 normally intron-containing tRNAs, indicating this repair pathway does not have additional essential functions. Expression of intronless tRNAs fails to rescue the growth of cells with deletions in components of the SEN complex, implying an additional essential role for the splicing endonuclease. The trl1DELTA and tpt1DELTA mutants accumulate tRNA and HAC1 splicing intermediates indicative of RNA repair defects and are hypersensitive to drugs that inhibit translation. tpt1DELTA mutants grow in the presence of tunicamycin despite reduced accumulation of spliced HAC1 mRNA, while failure to induce the unfolded protein response occurs in trl1DELTA cells grown with tunicamycin is lethal owing to their inability to ligate HAC1 after its cleavage by Ire1. Tpt1DELTA phenotype, overview
H117A
-
colony size indistinguishable from that of wild-type TPT1 strain
H142A
-
colony size indistinguishable from that of wild-type TPT1 strain
H90A
-
colony size indistinguishable from that of wild-type TPT1 strain
S91A
-
colony size indistinguishable from that of wild-type TPT1 strain
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20Ā°C, Tris buffer, pH 7.5, 50% glycerol
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by Blue Sepharose column chromatography
His6-tagged wild-type RslTpt1 and mutant R16A/H17A/R64A/R119A RslTpt1 from Escherichia coli strain L21(DE3)-CodonPlus by nickel affinity chromatography, ultrafiltration, and gel filtration
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immobilized metal ion affinity chromatography, > 80% purified by SDS-PAGE
-
KptA-His6 10% purified by sonication, immobilized metal ion chromatography, centrifugation
-
Ni-agarose chromatography
partially purified
partially purified, GST-Tpt1 fusion protein purified by glutahthione agarose chromatography
-
purified 28000fold by Orange A Sepharose column, 4fold less pure by streamlined purification procedure
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
Tpt1-His6 50% purified by sonication, immobilized metal ion chromatography, centrifugation
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recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli as a His-6 fusion, expression in Saccharomyces cerevisiae tpt1 mutant
expression in Saccharomyces cerevisiae tpt1 mutant strain Y2, the human TRPT1 gene could complement this mutation
expression in Saccharomyces cerevisiae tpt1 mutant strain Y2, the wild-type yeast TPT1 could complement this mutation
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expression in Saccharomyces cerevisiae tpt1 mutants
Fusion of the coding region of the splicing enzyme in-frame to the amino-terminus of the green fluorescent protein (GFP). Full-length 2'-phosphotransferase cDNA (289 aa) and a short version of the same polypeptide starting with the second methionine at position 33 are fused to the coding region of GFP. Additionally, the N-terminal sequence of 97 amino acids derived from the 2'-phosphotransferase is directly fused to GFP.
-
gene CTHT_0025470, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene kptA, encoded in an operon-like cluster with genes encoding RNA polymerase, RNA ligase, and the Hen1/Pnkp RNA repairsystem reported to repair ribotoxin-degraded tRNAs in vitro
gene kptA, genomic organization, comparisons
gene kptA, genomic organization, comparisons, the gene kpta neighborhood includes the genes coding for: (i) the enzyme Nam phosphoribo-syltransferase (NadV), involved in the recycling to NAD of Nam, thepyridine product of the KptA-catalyzed reaction, (ii) the orthologue of the yeast ADPR-1-P phosphatase, implicated in the conversionto ADPR of the adenylylic product, (iii) the enzyme ADPR diphosphatase (ADPRP), responsible for ADPR hydrolysis to AMPand R5P, and (iv) the enzyme PRPP synthetase, which catalyzes PRPP formation from ATP and ribose 5-phosphate
gene kptA, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene TPT1, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
the enzyme RslTpt1 is encoded within a putative RNA repair gene cluster, recombinant expression of wild-type RslTpt1 and mutant R16A/H17A/R64A/R119A RslTpt1 in Saccharomyces cerevisiae tpt1DELTA haploid strain YBS501, in which the TPT1 ORF is deleted and replaced by LEU2 and which is dependent for viability on the p360-TPT1 plasmid (CEN URA3 SceTPT1), recombiant expression of His6-tagged wild-type RslTpt1 and mutant R16A/H17A/R64A/R119A RslTpt1 in Escherichia coli strain L21(DE3)-CodonPlus
-
The murine Trpt1 gene is targeted in E14 ES cells with a positive/negative selection vector. Trpt1 gene is disrupted by homologous recombination in ES cells, deleting exons 3, 4, and part of exon 5 that encode amino acids 48-173. Clones from two individually selected heterozygous ES cell lines are injected into blastocysts and the resultant founder chimeras bred to obtain two lines of Trpt1+/- and Trpt1-/-mice that are both viable and healthy and are normally fertile. Cell culture: Trpt1+/+ and Trpt1-/-cell lines are obtained by serial passage of SV40-T-antigen transfected mouse embryonic fibroblasts.
-
expression in Escherichia coli as a His-6 fusion, expression in Saccharomyces cerevisiae tpt1 mutant
-
expression in Escherichia coli as a His-6 fusion, expression in Saccharomyces cerevisiae tpt1 mutant
-
gene kptA, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene kptA, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene kptA, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene kptA, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
Inhibitors of Tpt1p might prove useful as selective antifungal agents.
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Culver, G.M.; McCraith, S.M.; Consaul, S.A.; Stanford, D.R.; Phizicky, E.M.
A 2'-phosphotransferase implicated in tRNA splicing is essential in Saccharomyces cerevisiae
J. Biol. Chem.
272
13203-13210
1997
Saccharomyces cerevisiae, Saccharomyces cerevisiae (Q12272), Escherichia coli, Homo sapiens, Mus musculus, Schizosaccharomyces pombe
brenda
Steiger, M.A.; Kierzek, R.; Turner, D.H.; Phizicky, E.M.
Substrate recognition by a yeast 2'-phosphotransferase involved in tRNA splicing and by its Escherichia coli homolog
Biochemistry
40
14098-14105
2001
Saccharomyces cerevisiae, Escherichia coli
brenda
Hu, Q.D.; Lu, H.; Huo, K.; Ying, K.; Li, J.; Xie, Y.; Mao, Y.; Li, Y.Y.
A human homolog of the yeast gene encoding tRNA 2'-phosphotransferase: cloning, characterization and complementation analysis
Cell. Mol. Life Sci.
60
1725-1732
2003
Arabidopsis thaliana, Archaeoglobus fulgidus, Saccharomyces cerevisiae, Clostridium perfringens, Escherichia coli, Fusobacterium nucleatum, Homo sapiens, Homo sapiens (Q86TN4), Methanopyrus kandleri, Mus musculus, Rattus norvegicus, Schizosaccharomyces pombe, Streptomyces coelicolor
brenda
Mc Craith, S.M.; Phizicky, E.M.
An enzyme from Saccharomyces cerevisiae uses NAD+ to transfer the splice junction 2'-phosphate from ligated tRNA to an acceptor molecule
J. Biol. Chem.
266
11986-11992
1991
Saccharomyces cerevisiae
brenda
Zillman, M.; Gorovsky, M.A.; Phizicky, E.M.
HeLa cells contain a 2'-phosphate-specific phosphotransferase similar to a yeast enzyme implicated in tRNA splicing
J. Biol. Chem.
267
10289-10294
1992
Saccharomyces cerevisiae, Homo sapiens
brenda
Spinelli, S.L.; Kierzek, R.; Turner, D.H.; Phizicky, E.M.
Transient ADP-ribosylation of a 2'-phosphate implicated in its removal from ligated tRNA during splicing in yeast
J. Biol. Chem.
274
2637-2644
1999
Saccharomyces cerevisiae, Escherichia coli, Mus musculus
brenda
Kato-Murayama, M.; Bessho, Y.; Shirouzu, M.; Yokoyama, S.
Crystal structure of the RNA 2'-phosphotransferase from Aeropyrum pernix K1
J. Mol. Biol.
348
295-305
2005
Aeropyrum pernix, Arabidopsis thaliana, Archaeoglobus fulgidus, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Methanosarcina mazei, Pseudomonas aeruginosa, Pyrococcus horikoshii
brenda
Kierzek, R.; Steiger, M.A.; Spinelli, S.L.; Turner, D.H.; Phizicky, E.M.
The chemical synthesis of oligoribonucleotides with selectively placed 2'-O-phosphates
Nucleosides Nucleotides Nucleic Acids
19
917-933
2000
Saccharomyces cerevisiae
brenda
Spinelli, S.L.; Malik, H.S.; Consaul, S.A.; Phizicky, E.M.
A functional homolog of a yeast tRNA splicing enzyme is conserved in higher eukaryotes and in Escherichia coli
Proc. Natl. Acad. Sci. USA
95
14136-14141
1998
Arabidopsis thaliana, Archaeoglobus fulgidus, Saccharomyces cerevisiae, Candida albicans, Escherichia coli, Mus musculus, no activity in Bacillus subtilis, no activity in Haemophilus influenzae, no activity in Mycoplasma genitalium, Pseudomonas aeruginosa, Pyrococcus horikoshii, Schizosaccharomyces pombe, no activity in Helicobacter pylori
brenda
Sawaya, R.; Schwer, B.; Shuman, S.
Structure-function analysis of the yeast NAD+-dependent tRNA 2'-phosphotransferase Tpt1
RNA
11
107-113
2005
Aeropyrum pernix, Archaeoglobus fulgidus, Saccharomyces cerevisiae, Clostridium perfringens, Drosophila melanogaster, Escherichia coli, Homo sapiens, Leishmania major, Nostoc punctiforme, Pyrococcus horikoshii, Schizosaccharomyces pombe, Trypanosoma cruzi
brenda
Steiger, M.A.; Jackman, J.E.; Phizicky, E.M.
Analysis of 2'-phosphotransferase (Tpt1p) from Saccharomyces cerevisiae: evidence for a conserved two-step reaction mechanism
RNA
11
99-106
2005
Saccharomyces cerevisiae
brenda
Spinelli, S.L.; Consaul, S.A.; Phizicky, E.M.
A conditional lethal yeast phosphotransferase (tpt1) mutant accumulates tRNAs with a 2'-phosphate and an undermodified base at the splice junction
RNA
3
1388-1400
1997
Saccharomyces cerevisiae, Escherichia coli
brenda
Englert, M.; Latz, A.; Becker, D.; Gimple, O.; Beier, H.; Akama, K.
Plant pre-tRNA splicing enzymes are targeted to multiple cellular compartments
Biochimie
89
1351-1365
2007
Arabidopsis thaliana
brenda
Lackey, J.G.; Ron, D.; Damha, M.J.; Harding, H.P.
Toward the discovery of new antifungal agents: the design and validation of a novel 2P-RNA probe and high throughput screening assay against 2-phosphotransferase Tpt1p
Nucleic Acids Symp. Ser.
52
475-476
2008
yeasts
brenda
Harding, H.P.; Lackey, J.G.; Hsu, H.C.; Zhang, Y.; Deng, J.; Xu, R.M.; Damha, M.J.; Ron, D.
An intact unfolded protein response in Trpt1 knockout mice reveals phylogenic divergence in pathways for RNA ligation
RNA
14
225-232
2008
Mus musculus
brenda
Sorci, L.; Ruggieri, S.; Raffaelli, N.
NAD homeostasis in the bacterial response to DNA/RNA damage
DNA Repair
23
17-26
2014
Saccharomyces cerevisiae, Brachyspira hyodysenteriae (A0A3B6VB17), Flavobacterium johnsoniae (A5FLZ4), Herpetosiphon aurantiacus (A9B356), Delftia acidovorans (A9C0S5), Deinococcus deserti (C1CZ01), Catenulispora acidiphila (C7QAQ2), Sebaldella termitidis (D1APE3), Deinococcus gobiensis (H8GTD5), Fusobacterium nucleatum subsp. nucleatum (Q8R5N7), Agrobacterium tumefaciens (Q8U9Z2), Deinococcus radiodurans (Q9RRR1), Delftia acidovorans DSM 14801 (A9C0S5), Agrobacterium tumefaciens C58 / ATCC 33970 (Q8U9Z2), Brachyspira hyodysenteriae ATCC 49526 (A0A3B6VB17), Herpetosiphon aurantiacus DSM 785 (A9B356), Deinococcus gobiensis DSM 21396 (H8GTD5), Deinococcus radiodurans ATCC 13939 (Q9RRR1), Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847 (Q8R5N7), Deinococcus deserti DSM 17065 (C1CZ01), Sebaldella termitidis ATCC 33386 (D1APE3)
brenda
Munir, A.; Banerjee, A.; Shuman, S.
NAD+-dependent synthesis of a 5-phospho-ADP-ribosylated RNA/DNA cap by RNA 2-phosphotransferase Tpt1
Nucleic Acids Res.
46
9617-9624
2018
Runella slithyformis, Hungateiclostridium thermocellum (A3DJX6), Chaetomium thermophilum (G0S5Z5), Archaeoglobus fulgidus (O29841), Pyrococcus horikoshii (O57899), Saccharomyces cerevisiae (Q12272), Homo sapiens (Q86TN4), Aeropyrum pernix (Q9YFP5), Aeropyrum pernix, Aeropyrum pernix ATCC 700893 (Q9YFP5), Aeropyrum pernix DSM 11879 (Q9YFP5), Archaeoglobus fulgidus NBRC 100126 (O29841), Archaeoglobus fulgidus ATCC 49558 (O29841), Pyrococcus horikoshii DSM 12428 (O57899), Hungateiclostridium thermocellum NCIMB 10682 (A3DJX6), Hungateiclostridium thermocellum NBRC 103400 (A3DJX6), Aeropyrum pernix JCM 9820 (Q9YFP5), Pyrococcus horikoshii NBRC 100139 (O57899), Hungateiclostridium thermocellum JCM 9322 (A3DJX6), Hungateiclostridium thermocellum ATCC 27405 (A3DJX6), Pyrococcus horikoshii JCM 9974 (O57899), Chaetomium thermophilum CBS 144.50 (G0S5Z5), Hungateiclostridium thermocellum VPI 7372 (A3DJX6), Archaeoglobus fulgidus VC-16 (O29841), Aeropyrum pernix NBRC 100138 (Q9YFP5), Pyrococcus horikoshii ATCC 700860 (O57899), Chaetomium thermophilum IMI 039719 (G0S5Z5), Chaetomium thermophilum DSM 1495 (G0S5Z5), Hungateiclostridium thermocellum NRRL B-4536 (A3DJX6), Pyrococcus horikoshii OT-3 (O57899), Hungateiclostridium thermocellum DSM 1237 (A3DJX6), Archaeoglobus fulgidus JCM 9628 (O29841)
brenda
Munir, A.; Abdullahu, L.; Damha, M.J.; Shuman, S.
Two-step mechanism and step-arrest mutants of Runella slithyformis NAD+-dependent tRNA 2'-phosphotransferase Tpt1
RNA
24
1144-1157
2018
Runella slithyformis, Runella slithyformis ATCC 49304
brenda
Cherry, P.D.; White, L.K.; York, K.; Hesselberth, J.R.
Genetic bypass of essential RNA repair enzymes in budding yeast
RNA
24
313-323
2018
Saccharomyces cerevisiae (Q12272)
brenda
Dantuluri, S.; Abdullahu, L.; Munir, A.; Katolik, A.; Damha, M.J.; Shuman, S.
Substrate analogs that trap the 2'-phospho-ADP-ribosylated RNA intermediate of the Tpt1 (tRNA 2'-phosphotransferase) reaction pathway
RNA
26
373-381
2020
Runella slithyformis, Hungateiclostridium thermocellum (A3DJX6), Chaetomium thermophilum (G0S5Z5), Homo sapiens (Q86TN4), Hungateiclostridium thermocellum NCIMB 10682 (A3DJX6), Hungateiclostridium thermocellum NBRC 103400 (A3DJX6), Hungateiclostridium thermocellum JCM 9322 (A3DJX6), Hungateiclostridium thermocellum ATCC 27405 (A3DJX6), Chaetomium thermophilum CBS 144.50 (G0S5Z5), Hungateiclostridium thermocellum VPI 7372 (A3DJX6), Chaetomium thermophilum IMI 039719 (G0S5Z5), Chaetomium thermophilum DSM 1495 (G0S5Z5), Hungateiclostridium thermocellum NRRL B-4536 (A3DJX6), Hungateiclostridium thermocellum DSM 1237 (A3DJX6)
brenda
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