2.7.1.160: 2'-phosphotransferase
This is an abbreviated version!
For detailed information about 2'-phosphotransferase, go to the full flat file.
Word Map on EC 2.7.1.160
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2.7.1.160
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2'-phosphate
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junction
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adp-ribose
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adp-ribosylation
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2.7.1.23
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phosphodiester
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2'-phosphorylated
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pre-trnas
- 2.7.1.160
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2'-phosphate
- junction
- adp-ribose
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adp-ribosylation
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2.7.1.23
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phosphodiester
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2'-phosphorylated
- pre-trnas
Reaction
Synonyms
2'-phosphotransferase, ApeTpt1, AtPt, CTHT_0025470, HeLa cell 2'-phosphotransferase, human TRPT1, KptA, kptA1, mTPT1, NAD+-dependent 2'-phosphotransferase, NAD-dependent RNA 2'-phosphotransferase, RNA 2'-phosphotransferase, RslTpt1, Tpt1, Tpt1p, tRNA 2'-phosphotransferase, Trpt1, yeast 2'-phosphotransferase
ECTree
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Inhibitors
Inhibitors on EC 2.7.1.160 - 2'-phosphotransferase
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ApGpApUpUpUpApC
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oligonucleotide, which lacks secondary structure and has no terminal phosphate
PS-2'-FANA oligonucleotides
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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
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PS-DNA oligonucleotides
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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
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[pre-tRNA]
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intron-containing yeast [pre-tRNA], which has the same structure as mature yeast [tRNA], except in the region of the intron
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[tRNA]
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mature Escherichia coli [tRNA], has canonical tRNA structue
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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
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2'-fluoroarabinose
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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
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2'-fluoroarabinose
Thermochaetoides thermophila
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
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human Tpt1 effects no detectable reaction of the 2'-phosphate RNA substrate in the presence of 0.05 mM ara-2''F-NAD+
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ara-2''F-NAD+
Thermochaetoides thermophila
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
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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
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arabinose-2'-phosphate
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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
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arabinose-2'-phosphate
Thermochaetoides thermophila
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
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analysis of chemically modified nucleic acid substrates for activity with bacterial Tpt1 enzymes
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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
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additional information
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analysis of chemically modified nucleic acid substrates for activity with bacterial Tpt1 enzymes
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