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Literature summary for 2.7.1.160 extracted from

  • 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 (2020), RNA, 26, 373-381 .
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
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 Acetivibrio thermocellus
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 Runella slithyformis
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 Thermochaetoides thermophila
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+ Homo sapiens
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 Thermochaetoides thermophila
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 Acetivibrio thermocellus
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 Runella slithyformis
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 Thermochaetoides thermophila
additional information analysis of chemically modified nucleic acid substrates for activity with bacterial Tpt1 enzymes Acetivibrio thermocellus
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 Homo sapiens
additional information analysis of chemically modified nucleic acid substrates for activity with bacterial Tpt1 enzymes Runella slithyformis
additional information analysis of chemically modified nucleic acid substrates for activity with bacterial Tpt1 enzymes Thermochaetoides thermophila
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 Runella slithyformis
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 Runella slithyformis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2'-phospho-[ligated tRNA] + NAD+ Homo sapiens
-
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+ Runella slithyformis
-
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+ Acetivibrio thermocellus
-
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+ Thermochaetoides thermophila
-
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+ Thermochaetoides thermophila IMI 039719
-
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+ Acetivibrio thermocellus DSM 1237
-
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+ Thermochaetoides thermophila DSM 1495
-
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+ Acetivibrio thermocellus JCM 9322
-
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+ Acetivibrio thermocellus NBRC 103400
-
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+ Acetivibrio thermocellus ATCC 27405
-
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+ Acetivibrio thermocellus VPI 7372
-
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+ Thermochaetoides thermophila CBS 144.50
-
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+ Acetivibrio thermocellus NCIMB 10682
-
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+ Acetivibrio thermocellus NRRL B-4536
-
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?

Organism

Organism UniProt Comment Textmining
Acetivibrio thermocellus A3DJX6 Clostridium thermocellum
-
Acetivibrio thermocellus ATCC 27405 A3DJX6 Clostridium thermocellum
-
Acetivibrio thermocellus DSM 1237 A3DJX6 Clostridium thermocellum
-
Acetivibrio thermocellus JCM 9322 A3DJX6 Clostridium thermocellum
-
Acetivibrio thermocellus NBRC 103400 A3DJX6 Clostridium thermocellum
-
Acetivibrio thermocellus NCIMB 10682 A3DJX6 Clostridium thermocellum
-
Acetivibrio thermocellus NRRL B-4536 A3DJX6 Clostridium thermocellum
-
Acetivibrio thermocellus VPI 7372 A3DJX6 Clostridium thermocellum
-
Homo sapiens Q86TN4
-
-
Runella slithyformis
-
-
-
Thermochaetoides thermophila G0S5Z5
-
-
Thermochaetoides thermophila CBS 144.50 G0S5Z5
-
-
Thermochaetoides thermophila DSM 1495 G0S5Z5
-
-
Thermochaetoides thermophila IMI 039719 G0S5Z5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2'-phospho-[ligated tRNA] + NAD+
-
Homo sapiens mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+
-
Runella slithyformis mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+
-
Acetivibrio thermocellus mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+
-
Thermochaetoides thermophila mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+
-
Thermochaetoides thermophila IMI 039719 mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+
-
Acetivibrio thermocellus DSM 1237 mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+
-
Thermochaetoides thermophila DSM 1495 mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+
-
Acetivibrio thermocellus JCM 9322 mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+
-
Acetivibrio thermocellus NBRC 103400 mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+
-
Acetivibrio thermocellus ATCC 27405 mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+
-
Acetivibrio thermocellus VPI 7372 mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+
-
Thermochaetoides thermophila CBS 144.50 mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+
-
Acetivibrio thermocellus NCIMB 10682 mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
2'-phospho-[ligated tRNA] + NAD+
-
Acetivibrio thermocellus NRRL B-4536 mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
-
?
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 Thermochaetoides thermophila ?
-
-
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 Runella slithyformis ?
-
-
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 Homo sapiens ?
-
-
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 Acetivibrio thermocellus ?
-
-
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 Thermochaetoides thermophila IMI 039719 ?
-
-
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 Acetivibrio thermocellus DSM 1237 ?
-
-
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 Thermochaetoides thermophila DSM 1495 ?
-
-
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 Acetivibrio thermocellus JCM 9322 ?
-
-
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 Acetivibrio thermocellus NBRC 103400 ?
-
-
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 Acetivibrio thermocellus ATCC 27405 ?
-
-
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 Acetivibrio thermocellus VPI 7372 ?
-
-
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 Thermochaetoides thermophila CBS 144.50 ?
-
-
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 Acetivibrio thermocellus NCIMB 10682 ?
-
-
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 Acetivibrio thermocellus NRRL B-4536 ?
-
-

Synonyms

Synonyms Comment Organism
Tpt1
-
Homo sapiens
Tpt1
-
Runella slithyformis
Tpt1
-
Acetivibrio thermocellus
Tpt1
-
Thermochaetoides thermophila
tRNA 2'-phosphotransferase
-
Homo sapiens
tRNA 2'-phosphotransferase
-
Runella slithyformis
tRNA 2'-phosphotransferase
-
Acetivibrio thermocellus
tRNA 2'-phosphotransferase
-
Thermochaetoides thermophila

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens
37
-
assay at Runella slithyformis
37
-
assay at Acetivibrio thermocellus
37
-
assay at Thermochaetoides thermophila

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Homo sapiens
7.5
-
assay at Runella slithyformis
7.5
-
assay at Acetivibrio thermocellus
7.5
-
assay at Thermochaetoides thermophila

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Homo sapiens
NAD+
-
Runella slithyformis
NAD+
-
Acetivibrio thermocellus
NAD+
-
Thermochaetoides thermophila

General Information

General Information Comment Organism
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 Homo sapiens
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 Runella slithyformis
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 Acetivibrio thermocellus
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 Thermochaetoides thermophila
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 Homo sapiens
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 Thermochaetoides thermophila
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 Acetivibrio thermocellus
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 Runella slithyformis
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 Runella slithyformis
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 Acetivibrio thermocellus
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 Thermochaetoides thermophila
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 Homo sapiens