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Information on EC 2.7.1.160 - 2'-phosphotransferase and Organism(s) Homo sapiens and UniProt Accession Q86TN4

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IUBMB 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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Homo sapiens
UNIPROT: Q86TN4
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
2'-phosphotransferase, trpt1, rsltpt1, tpt1p, trna 2'-phosphotransferase, human trpt1, apetpt1, rna 2'-phosphotransferase, yeast 2'-phosphotransferase, nad+-dependent 2'-phosphotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
human TRPT1
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RNA 2'-phosphotransferase
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tRNA 2'-phosphotransferase
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HeLa cell 2'-phosphotransferase
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RNA 2'-phosphotransferase
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tRNA 2'-phosphotransferase
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PATHWAY SOURCE
PATHWAYS
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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].
CAS REGISTRY NUMBER
COMMENTARY hide
126905-00-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
show the reaction diagram
-
-
-
?
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP ribose-1'',2''-phosphate + nicotinamide + H2O
show the reaction diagram
-
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
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-
?
additional information
?
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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
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2'-phospho-[ligated tRNA] + NAD+
mature tRNA + ADP-ribose 1'',2''-phosphate + nicotinamide
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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+
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Formamide
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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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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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swissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
high level of TRPT1 transcript
Manually annotated by BRENDA team
intermediate level of TRPT1 transcript
Manually annotated by BRENDA team
intermediate level of TRPT1 transcript
Manually annotated by BRENDA team
low level of TRPT1 transcript
Manually annotated by BRENDA team
highest level of TRPT1 transcript
Manually annotated by BRENDA team
low level of TRPT1 transcript
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
physiological function
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TRPT1_HUMAN
253
0
27742
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27800
estimated theorethical molecular mass of the deduced translation product
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20, Tris-HCl buffer, pH. 8.0, 50% glycerol, several months
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-80°C, Tris-HCl buffer, pH 8.0, 20% glycerol
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
partially purified by chromatography on heparin-agarose
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae tpt1 mutant strain Y2, the human TRPT1 gene could complement this mutation
gene TPT1, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
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
Escherichia coli, Homo sapiens, Mus musculus, Saccharomyces cerevisiae, Saccharomyces cerevisiae (Q12272), Schizosaccharomyces pombe
Manually annotated by BRENDA team
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, Clostridium perfringens, Escherichia coli, Fusobacterium nucleatum, Homo sapiens, Homo sapiens (Q86TN4), Methanopyrus kandleri, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Streptomyces coelicolor
Manually annotated by BRENDA team
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
Homo sapiens, Saccharomyces cerevisiae
Manually annotated by BRENDA team
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, Escherichia coli, Homo sapiens, Methanosarcina mazei, Pseudomonas aeruginosa, Pyrococcus horikoshii, Saccharomyces cerevisiae
Manually annotated by BRENDA team
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, Clostridium perfringens, Drosophila melanogaster, Escherichia coli, Homo sapiens, Leishmania major, Nostoc punctiforme, Pyrococcus horikoshii, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Trypanosoma cruzi
Manually annotated by BRENDA team
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
Acetivibrio thermocellus (A3DJX6), Acetivibrio thermocellus ATCC 27405 (A3DJX6), Acetivibrio thermocellus DSM 1237 (A3DJX6), Acetivibrio thermocellus JCM 9322 (A3DJX6), Acetivibrio thermocellus NBRC 103400 (A3DJX6), Acetivibrio thermocellus NCIMB 10682 (A3DJX6), Acetivibrio thermocellus NRRL B-4536 (A3DJX6), Acetivibrio thermocellus VPI 7372 (A3DJX6), Aeropyrum pernix (Q9YFP5), Aeropyrum pernix, Aeropyrum pernix ATCC 700893 (Q9YFP5), Aeropyrum pernix DSM 11879 (Q9YFP5), Aeropyrum pernix JCM 9820 (Q9YFP5), Aeropyrum pernix NBRC 100138 (Q9YFP5), Archaeoglobus fulgidus (O29841), Archaeoglobus fulgidus ATCC 49558 (O29841), Archaeoglobus fulgidus JCM 9628 (O29841), Archaeoglobus fulgidus NBRC 100126 (O29841), Archaeoglobus fulgidus VC-16 (O29841), Homo sapiens (Q86TN4), Pyrococcus horikoshii (O57899), Pyrococcus horikoshii ATCC 700860 (O57899), Pyrococcus horikoshii DSM 12428 (O57899), Pyrococcus horikoshii JCM 9974 (O57899), Pyrococcus horikoshii NBRC 100139 (O57899), Pyrococcus horikoshii OT-3 (O57899), Runella slithyformis, Saccharomyces cerevisiae (Q12272), Thermochaetoides thermophila (G0S5Z5), Thermochaetoides thermophila CBS 144.50 (G0S5Z5), Thermochaetoides thermophila DSM 1495 (G0S5Z5), Thermochaetoides thermophila IMI 039719 (G0S5Z5)
Manually annotated by BRENDA team
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
Acetivibrio thermocellus (A3DJX6), Acetivibrio thermocellus ATCC 27405 (A3DJX6), Acetivibrio thermocellus DSM 1237 (A3DJX6), Acetivibrio thermocellus JCM 9322 (A3DJX6), Acetivibrio thermocellus NBRC 103400 (A3DJX6), Acetivibrio thermocellus NCIMB 10682 (A3DJX6), Acetivibrio thermocellus NRRL B-4536 (A3DJX6), Acetivibrio thermocellus VPI 7372 (A3DJX6), Homo sapiens (Q86TN4), Runella slithyformis, Thermochaetoides thermophila (G0S5Z5), Thermochaetoides thermophila CBS 144.50 (G0S5Z5), Thermochaetoides thermophila DSM 1495 (G0S5Z5), Thermochaetoides thermophila IMI 039719 (G0S5Z5)
Manually annotated by BRENDA team