6.5.1.3 (deoxyribonucleotide)n - Methanothermobacter thermautotrophicus circular (deoxyribonucleotide)n - ? 399185 6.5.1.3 (ribonucleotide)n - Methanothermobacter thermautotrophicus circular (ribonucleotide)n - ? 399213 6.5.1.3 5'-adenylated cytidine 5',3'-bisphosphate + diguanosine tetraphosphate - Tequatrovirus T4 Gp4GpCp + pCpGp4GpCp - ? 369211 6.5.1.3 8-Bromoadenosine 5'-triphosphate + (ribonucleotide)n + (ribonucleotide)m - Tequatrovirus T4 8-Bromoadenosine monophosphate + (ribonucleotide)n+m - ? 816 6.5.1.3 8-Sulfoadenosine 5'-triphosphate + (ribonucleotide)n + (ribonucleotide)m - Tequatrovirus T4 8-Sulfoadenosinemonophosphate + phosphate + (ribonucleotide)n+m - ? 815 6.5.1.3 ATP + (2E,6E)-farnesyl diphosphate assay contains pyruvate kinase, phosphoenolpyruvate and pyrophosphatase to recover ATP Tequatrovirus T4 (2E,6E)-farnesyl-triphospho(5')adenosine + diphosphate - ir 411651 6.5.1.3 ATP + (2E,6E)-farnesyl triphosphate assay contains pyruvate kinase, phosphoenolpyruvate and pyrophosphatase to recover ATP Tequatrovirus T4 (2E,6E)-farnesyl-tetraphospho(5')adenosine + diphosphate - ir 411652 6.5.1.3 ATP + (deoxyribonucleotide)n - Methanothermobacter thermautotrophicus adenylyl-(deoxyribonucleotide)n + diphosphate - ? 399990 6.5.1.3 ATP + (ribonucleotide)n - Methanothermobacter thermautotrophicus adenylyl-(ribonucleotide)n + diphosphate - ? 399994 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m - Homo sapiens AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m - Triticum aestivum AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m - Trypanosoma brucei AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m - Tequatrovirus T4 AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m - Tequatrovirus T4 AMP + diphosphate + (ribonucleotide)n+m - r 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m - Leishmania tarentolae AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m - synthetic construct AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m - Rhodothermus phage RM378 AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m - Vibrio phage KVP40 AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m - Branchiostoma floridae AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m poly(A) containing 5'-P-2,3-cyclic P termini Triticum aestivum AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m RNA substrates containing a 5'-phosphate terminus at one end and either a 2',3'-cyclic phosphate or a 2'-phosphate terminus at the other end. In the latter case the reaction is about 30% as active as with the cyclic derivative Triticum aestivum AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m participates in an in vitro splicing of yeast transfer RNA precursors containing intervening sequences. Covalently ligates tRNA5' and 3' half-molecules produced by a yeast endonuclease Triticum aestivum AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m conversion of linear polyribonucleotides into covalently closed circles, formation of a 2'-phosphomonoester,3',5'-phosphodiester linkage Triticum aestivum AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m converts linear molecules of polyriboadenylate to circular form by the intramolecular covalent linkage of the 5'-phosphate end to the 3'-hydroxyl terminus Tequatrovirus T4 AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m formation of a phosphodiester bond between a 5'-PO4-terminated oligonucleotide and a 3'-OH terminated oligonucleotide. Intramolecular formation of single-stranded circles with longer oligonucleotides of the type pAp(Ap)nAOH, where n is about 15 or greater. Intermolecular joining of pAp(Ap)3AOH, where the 5'-PO4-terminated oligonucleotide is short enough to prevent apposition of its 3' and 5' ends, to UpUpUOH Tequatrovirus T4 AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m cylization of poly(A) Tequatrovirus T4 AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m the best substrate is [5'-P]polyriboadenylate Tequatrovirus T4 AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m ligates two substrate RNAs, promoting the attack of the 3'-hydroxyl of one substrate upon the 5'-triphosphate of the other substrate with release of diphosphate, reverse of ligation has been detected, but very inefficient, not saturable by soluble amounts of diphosphate synthetic construct AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m only the di-magnesium-coordinated form Mg2ATP0 reacts with the enzyme, forming the covalent complex E-AMP, the reverse reaction, ATP synthesis, occurs between the mono-magnesium-coordinated diphosphate from MgP2O72- and the enzyme-MgAMP complex Tequatrovirus T4 AMP + diphosphate + (ribonucleotide)n+m - r 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m catalyzes RNA end-joining Vibrio phage KVP40 AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m catalyzes the transfer of AMP from the E-AMP complex to diverse compounds, generating the product indicated between parentheses, ATP(Ap4A), NTP (Ap4N), P3 or P4 (p4A or p5A), ADP (Ap3A) Tequatrovirus T4 AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m participates in repair, splicing and editing pathways, reseals broken RNAs or alters their primary structure, catalyzes intramolecular and intermolecular RNA strand joining through ligase-adenylate and RNA adenylate intermediates Tequatrovirus T4 AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m RNA editing, essential for proliferation of Trypanosoma brucei Trypanosoma brucei AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m RNA editing, posttranscriptional insertion and deletion of uridylate residues in mitochondrial transcripts Trypanosoma brucei AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m RNA editing, posttranscriptional process by which uridine residues are added and deleted from mitochondrial mRNAs Trypanosoma brucei AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m RNA editing, posttranscriptional RNA processing in which uridylate residues are inserted into and deleted from pre-mRNAs to create start and stop codons, also acts to reseal mRNAs cleaved at incorrect sites Trypanosoma brucei AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m RNA editing, unique U insertion and U deletion process, involves cycles of pre-mRNA cleavage, terminal U addition or U removal, and religation, band IV is the RNA editing ligase needed to seal in U deletion Trypanosoma brucei AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m RNA-editing Tequatrovirus T4 AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m the enzyme is essential for survival of both insect and bloodstream forms of the parasite Trypanosoma brucei AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m DraRnl seals 3'-OH/5'-PO4 RNA nicks in either a duplex RNA or an RNA:DNA hybrid, but it cannot seal 3'-OH/5'-PO4 DNA nicks Deinococcus radiodurans AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m neither dATP, GTP, CTP, nor UTP can substitute for ATP. RNA ligation at a 3'-OH/5'-PO4 nick in a double-stranded RNA or an RNA-DNA hybrid Tequatrovirus T4 AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m the TS2126 RNA ligase catalyzes both inter- and intra-molecular single-stranded DNA ligation to more than 50% completion in not more than a few hours at an elevated temperature, although favoring intramolecular ligation on RNA and single-stranded DNA substrates Phage TS2126 AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m the L1 ligase is regioselective for formation of the biologically relevant 5' to 3' phosphodiester bond rather than a 5' to 2' bond Enterobacteria phage L1 AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m Trl1 executes the end-healing and end-sealing steps of tRNA splicing, requires a 2'-PO4 end for tRNA splicing in vivo Saccharomyces cerevisiae AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m Rnl1 has an inherent specificity for sealing tRNA with a break in the anticodon loop. The tRNA specificity is imparted by the C domain Tequatrovirus T4 AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m T4 RNA ligase 1 can efficiently adenylate DNA oligos with 5' phosphate and 3' blocking group Escherichia coli AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m the kinetic mechanism of single-turnover nick sealing by T4 Rnl2-AMP is explored by using a rapid mix-quench method and the effects of 3'-OH mispairs and base damage lesions on the rates of nick 5'-adenylylation and phosphodiester synthesis is determined. With respect to the sealing of perfectly paired nicks the rates of step 2 catalysis are rapid (9.5-17.9/sec) and similar in magnitude to the step 3 rates (7.9-32/sec). Rnl2 is kinetically sensitive to all 3'-OH base mispairs Tequatrovirus T4 AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m - Leishmania tarentolae UC AMP + diphosphate + (ribonucleotide)n+m - ? 813 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m possibly involved in posttranscriptional RNA editing process of mitochondrial transcripts Leishmania tarentolae ? - ? 369239 6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m possibly involved in posttranscriptional RNA editing process of mitochondrial transcripts Leishmania tarentolae UC ? - ? 369239 6.5.1.3 ATP + (ribonucleotide)n-3'-hydroxyl + 5'-phospho-(ribonucleotide)m - Methanothermobacter thermautotrophicus (ribonucleotide)n+m + AMP + diphosphate - ? 444214 6.5.1.3 ATP + (ribonucleotide)n-3'-hydroxyl + 5'-phospho-(ribonucleotide)m - Pyrococcus horikoshii (ribonucleotide)n+m + AMP + diphosphate - ? 444214 6.5.1.3 ATP + (ribonucleotide)n-3'-hydroxyl + 5'-phospho-(ribonucleotide)m - Naegleria gruberi (ribonucleotide)n+m + AMP + diphosphate - ? 444214 6.5.1.3 ATP + (ribonucleotide)n-3'-hydroxyl + 5'-phospho-(ribonucleotide)m - Tequatrovirus T4 (ribonucleotide)n+m + AMP + diphosphate - ? 444214 6.5.1.3 ATP + (ribonucleotide)n-3'-hydroxyl + 5'-phospho-(ribonucleotide)m - Diplonema papillatum (ribonucleotide)n+m + AMP + diphosphate - ? 444214 6.5.1.3 ATP + (ribonucleotide)n-3'-hydroxyl + 5'-phospho-(ribonucleotide)m - Methanothermobacter thermautotrophicus ATCC 29096 (ribonucleotide)n+m + AMP + diphosphate - ? 444214 6.5.1.3 ATP + (RNA)n - synthetic construct ? - ? 454107 6.5.1.3 ATP + 5'-aaaCCAGUC RNA-DNA hybrid as substrate, chemical step is represented as irreversible, because reverse reaction, pyrophosphorolysis with formation of a triphosphate is 10000000-times slower than the forward reaction synthetic construct AMP + diphosphate + ? - ir 369204 6.5.1.3 ATP + 5'-phosphate termini of RNA - Triticum aestivum ? - ? 453791 6.5.1.3 ATP + ATP - Tequatrovirus T4 P1,P4-bis(5'-adenosyl) tetraphosphate + diphosphate - ? 369206 6.5.1.3 ATP + ATP - Tequatrovirus T4 P1,P3-bis(5'-adenosyl) triphosphate + ? - ? 369208 6.5.1.3 ATP + clodronate - Tequatrovirus T4 adenosine 5'-(beta,gamma-dichloromethylenetriphosphate) + ? - ? 387989 6.5.1.3 ATP + dimethylallyl diphosphate assay contains pyruvate kinase, phosphoenolpyruvate and pyrophosphatase to recover ATP Tequatrovirus T4 dimethylallyl-triphospho(5')adenosine + diphosphate - ir 411667 6.5.1.3 ATP + etidronate weak activity Tequatrovirus T4 ? - ? 388040 6.5.1.3 ATP + geranyl diphosphate assay contains pyruvate kinase, phosphoenolpyruvate and pyrophosphatase to recover ATP Tequatrovirus T4 geranyl-triphospho(5')adenosine + diphosphate - ir 411671 6.5.1.3 ATP + geranyl triphosphate assay contains pyruvate kinase, phosphoenolpyruvate and pyrophosphatase to recover ATP Tequatrovirus T4 geranyl-tetraphospho(5')adenosine + diphosphate - ir 411673 6.5.1.3 ATP + isopentenyl diphosphate assay contains pyruvate kinase, phosphoenolpyruvate and pyrophosphatase to recover ATP Tequatrovirus T4 adenosine 5'-isopentenyl triphosphate + diphosphate - ir 411675 6.5.1.3 ATP + isopentenyl triphosphate assay contains pyruvate kinase, phosphoenolpyruvate and pyrophosphatase to recover ATP Tequatrovirus T4 isopentenyl-tetraphospho(5')adenosine + diphosphate - ir 411678 6.5.1.3 ATP + methylenebisphosphonate - Tequatrovirus T4 adenosine 5'-(beta,gamma-methylenetriphosphate) + ? - ? 388094 6.5.1.3 ATP + RNA + 5'-aaCCAGUC DNA-RNA hybrid synthetic construct AMP + diphosphate + ? - ? 369205 6.5.1.3 ATP + [RNA ligase]-L-lysine - Methanothermobacter thermautotrophicus [RNA ligase]-N6-(5'-adenylyl)-L-lysine + diphosphate - ? 444268 6.5.1.3 ATP + [RNA ligase]-L-lysine - Pyrococcus horikoshii [RNA ligase]-N6-(5'-adenylyl)-L-lysine + diphosphate - ? 444268 6.5.1.3 ATP + [RNA ligase]-L-lysine - Naegleria gruberi [RNA ligase]-N6-(5'-adenylyl)-L-lysine + diphosphate - ? 444268 6.5.1.3 ATP + [RNA ligase]-L-lysine - Tequatrovirus T4 [RNA ligase]-N6-(5'-adenylyl)-L-lysine + diphosphate - ? 444268 6.5.1.3 ATP + [RNA ligase]-L-lysine - Methanothermobacter thermautotrophicus ATCC 29096 [RNA ligase]-N6-(5'-adenylyl)-L-lysine + diphosphate - ? 444268 6.5.1.3 ATPgammaS + ATP - Tequatrovirus T4 P1,P4-bis(5'-adenosyl) tetraphosphate + thiodiphosphate - ? 369210 6.5.1.3 dATP + (ribonucleotide)n + (ribonucleotide)m - Homo sapiens dAMP + phosphate + (ribonucleotide)n+m - ? 814 6.5.1.3 dATP + (ribonucleotide)n + (ribonucleotide)m - Triticum aestivum dAMP + phosphate + (ribonucleotide)n+m - ? 814 6.5.1.3 dATP + (ribonucleotide)n + (ribonucleotide)m - Leishmania tarentolae dAMP + phosphate + (ribonucleotide)n+m - ? 814 6.5.1.3 dATP + (ribonucleotide)n + (ribonucleotide)m at 20% the activity relative to ATP Tequatrovirus T4 dAMP + phosphate + (ribonucleotide)n+m - ? 814 6.5.1.3 dATP + (ribonucleotide)n + (ribonucleotide)m acts on single-stranded or double-stranded DNA molecules. Acts on very small pieces of ribonucleic acid, with 40mers being the probable upper size limit. The minimum size of the 5'-moiety is a ribonucleoside 3',5'-bisphosphate Tequatrovirus T4 dAMP + phosphate + (ribonucleotide)n+m - ? 814 6.5.1.3 dATP + (ribonucleotide)n + (ribonucleotide)m - Leishmania tarentolae UC dAMP + phosphate + (ribonucleotide)n+m - ? 814 6.5.1.3 GTP + ATP - Tequatrovirus T4 P1-(5'-adenosyl),P4-(5'-guanosyl) tetraphosphate + diphosphate - ? 369207 6.5.1.3 ITP + (ribonucleotide)n + (ribonucleotide)m - Tequatrovirus T4 IMP + phosphate + (ribonucleotide)n+m - ? 817 6.5.1.3 additional information joins single-stranded DNA molecules much less efficiently. Many of them approximate a well-defined consensus sequence Tequatrovirus T4 ? - ? 89 6.5.1.3 additional information RNA-stimulated exchange reaction between ATP and diphosphate Triticum aestivum ? - ? 89 6.5.1.3 additional information efficient ligation of single-stranded DNAs and RNAs Tequatrovirus T4 ? - ? 89 6.5.1.3 additional information synthesizes circular hammerhead ribozymes from oligonucleotides, small RNA molecules resistant to circuarization by other means can be efficiently circularized on a preparative scale using a suitable DNA template Tequatrovirus T4 ? - ? 89 6.5.1.3 additional information no activity with alendronate nor pamidronate Tequatrovirus T4 ? - ? 89 6.5.1.3 additional information the group I intron from cyanobacterium Anabaena sp. catalyzes phosphodiester bond formation using a triphosphate on the 5'-terminal nucleotide, much like protein polymerases and engineered ribozymes. In the process, this ribozyme forms a unique circular RNA that incorporates the exogenous guanosine cofactor added during self-splicing Anabaena sp. ? - ? 89 6.5.1.3 additional information enzyme does not discriminate between RNA and DNA for phosphodiester bond formation Methanothermobacter thermautotrophicus ? - ? 89 6.5.1.3 additional information intramolecular ligation of 5'-PO4 single-strand RNA to form a covalently closed circular RNA molecule through ligase-adenylylate and RNA-adenylylate intermediates AppRNA. At the optimal temperature of 65°C, AppRNA is predominantly ligated to a circular product. At 35°C, phosphodiester bond formation is suppressed and the majority of the AppRNA is deadenylylated Methanothermobacter thermautotrophicus ? - ? 89 6.5.1.3 additional information T4 RNA ligase possesses nick-joining activity in RNA/DNA hybrids against junctional matches/mismatches complementary to the RNA strand as a ligation template. When a junctional mismatch is present at the 30-terminal of RNA probe, the nick-joining activity of T4Rnl2 is inhibited Tequatrovirus T4 ? - ? 89 6.5.1.3 additional information the RNA ligase has a a strict requirement for RNA substrates with a 2'-phosphate terminus for the ligation of RNAs with 5'-phosphate and 3'-hydroxyl ends. RNA ligase forms a 2'-phosphomonoester-3',5'-phosphodiester junction Branchiostoma floridae ? - ? 89 6.5.1.3 additional information wheat RNA ligase can be dissected into three isolated domain enzymes that are responsible for its core ligase, 5'-kinase, and 2',3'-cyclic phosphate 3'-phosphodiesterase activities, respectively. A side reaction on 5'-tri/diphosphate RNAs is dependent on ATP, a 2'-phosphate-3'-hydroxyl end, and the ligase domain. Two RNA molecules having 5'-hydroxyl and 2',3'-cyclic monophosphate groups are ligated almost stoichiometrically after separate conversion of respective terminal phosphate states into reactive ones Triticum aestivum ? - ? 89 6.5.1.3 additional information wheat RNA ligase contains 5'-hydroxyl kinase, 2',3'-cyclic phosphate 3'-phosphodiesterase, and 5'-phosphate 2'-phosphate-3'-hydroxyl RNA ligase activities Triticum aestivum ? - ? 89 6.5.1.3 additional information RtcA is able of cyclizing a 2'-phosphate RNA end in high yield. The rate of 2'-phosphate cyclization by RtcA is five orders of magnitude slower than 3'-phosphate cyclization, notwithstanding that RtcA binds with similar affinity to RNA3'p and RNA2'p substrates Escherichia coli ? - ? 89 6.5.1.3 additional information the enzyme catalyzes an adenylation reaction that is specific for ATP and either ssDNA or RNA. It does not require synthesis of a template strand for adenylation. To achieve quantitative DNA adenylation, single turnover reaction condition with substrate to enzyme ratio 1:1 should be used Methanothermobacter thermautotrophicus ? - ? 89 6.5.1.3 additional information the enzyme catalyzes formation of phosphodiester bonds between the 5'-phosphate and 3'-hydroxyl termini of single-stranded RNAs. It can also react with RNA with a 3'-phosphate end to generate a 2',3'-cyclic phosphate. The enzyme can additionally remove adenosine from the 3'-terminus of the RNA to produce 3'-deadenylated RNA Methanothermobacter thermautotrophicus ? - ? 89 6.5.1.3 additional information the enzyme is unreactive with a 5'-32P-labeled single-strand 18-mer pDNA substrate Naegleria gruberi ? - ? 89 6.5.1.3 additional information the enzyme seals nicked 3'-OH/5'-PO4 duplexes in which the 3'-OH strand is RNA. The enzyme entails reaction with ATP to form a covalent enzyme-AMP intermediate, transfer of AMP to the nick 5'-PO4, and attack of the RNA 3'-OH on the adenylylated nick to form a 3'-5' phosphodiester Naegleria gruberi ? - ? 89