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Literature summary extracted from

  • Desai, K.K.; Cheng, C.L.; Bingman, C.A.; Phillips, G.N.; Raines, R.T.
    A tRNA splicing operon: Archease endows RtcB with dual GTP/ATP cofactor specificity and accelerates RNA ligation (2014), Nucleic Acids Res., 42, 3931-3942.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
6.5.1.8 Pyrococcus horikoshii O59245
-
-
6.5.1.8 Pyrococcus horikoshii DSM 12428 O59245
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.5.1.8 (ribonucleotide)10-3'-phosphate + 5'-hydroxy-(ribonucleotide)10 + dGTP in the absence of Archease, RtcB-catalyzed RNA ligation proceeds efficiently with GTP and substantially less efficiently with dGTP and ITP. Inclusion of Archease in ligation reaction mixtures enables efficient utilization of GTP, dGTP, ATP or ITP Pyrococcus horikoshii (ribonucleotide)20 + dGMP + diphosphate
-
 ?
6.5.1.8 (ribonucleotide)10-3'-phosphate + 5'-hydroxy-(ribonucleotide)10 + dGTP in the absence of Archease, RtcB-catalyzed RNA ligation proceeds efficiently with GTP and substantially less efficiently with dGTP and ITP. Inclusion of Archease in ligation reaction mixtures enables efficient utilization of GTP, dGTP, ATP or ITP Pyrococcus horikoshii DSM 12428 (ribonucleotide)20 + dGMP + diphosphate
-
 ?
6.5.1.8 (ribonucleotide)10-3'-phosphate + 5'-hydroxy-(ribonucleotide)10 + GTP in the absence of Archease, RtcB-catalyzed RNA ligation proceeds efficiently with GTP and substantially less efficiently with dGTP and ITP. Inclusion of Archease in ligation reaction mixtures enables efficient utilization of GTP, dGTP, ATP or ITP Pyrococcus horikoshii (ribonucleotide)20 + GMP + diphosphate
-
 ?
6.5.1.8 (ribonucleotide)10-3'-phosphate + 5'-hydroxy-(ribonucleotide)10 + GTP in the absence of Archease, RtcB-catalyzed RNA ligation proceeds efficiently with GTP and substantially less efficiently with dGTP and ITP. Inclusion of Archease in ligation reaction mixtures enables efficient utilization of GTP, dGTP, ATP or ITP Pyrococcus horikoshii DSM 12428 (ribonucleotide)20 + GMP + diphosphate
-
 ?
6.5.1.8 (ribonucleotide)10-3'-phosphate + 5'-hydroxy-(ribonucleotide)10 + ITP in the absence of Archease, RtcB-catalyzed RNA ligation proceeds efficiently with GTP and substantially less efficiently with dGTP and ITP. Inclusion of Archease in ligation reaction mixtures enables efficient utilization of GTP, dGTP, ATP or ITP Pyrococcus horikoshii (ribonucleotide)20 + IMP + diphosphate
-
 ?
6.5.1.8 (ribonucleotide)10-3'-phosphate + 5'-hydroxy-(ribonucleotide)10 + ITP in the absence of Archease, RtcB-catalyzed RNA ligation proceeds efficiently with GTP and substantially less efficiently with dGTP and ITP. Inclusion of Archease in ligation reaction mixtures enables efficient utilization of GTP, dGTP, ATP or ITP Pyrococcus horikoshii DSM 12428 (ribonucleotide)20 + IMP + diphosphate
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.5.1.8 0.00018
-
 (ribonucleotide)10-3'-phosphate pH 7.0, 70°C, ligation reaction Pyrococcus horikoshii
6.5.1.8 0.00055
-
 (ribonucleotide)10-3'-phosphate pH 7.0, 70°C, presence of archease, ligation reaction Pyrococcus horikoshii

General Information

EC Number General Information Comment Organism
6.5.1.8 physiological function archease and RtcB from Pyrococcus horikoshii function in tandem, with Archease altering the catalytic properties of the RNA ligase. Catalytic concentrations of archease are sufficient to activate RtcB, and Archease accelerates both the RNA 3'-P guanylylation and ligation steps. Archease can alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently. RtcB variants that have inactivating substitutions in the guanine-binding pocket can be rescued by the addition of archease. Substitution of the archease metal-binding residues drastically reduces archease-dependent activation of RtcB Pyrococcus horikoshii