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Literature summary extracted from

  • Maughan, W.; Shuman, S.
    Distinct contributions of enzymic functional groups to the 2',3'-cyclic phosphodiesterase, 3'-phosphate guanylylation, and 3'-ppG/5'-OH ligation steps of the Escherichia coli RtcB nucleic acid splicing pathway (2016), J. Bacteriol., 198, 1294-1304 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
6.5.1.8 C78A completely inactive Escherichia coli
6.5.1.8 D75A the mutation allows cyclic phosphodiester hydrolysis but cripples 3'-phosphate guanylylation Escherichia coli
6.5.1.8 H168A the mutant shows about 48% of 5'-OH-RNAp ligation activity compared to the wild type enzyme Escherichia coli
6.5.1.8 H185A the mutant shows 5'-OH-RNAp ligation activity similar to the wild type enzyme Escherichia coli
6.5.1.8 H281A the mutant is impaired in overall 5'-OH-RNAp and 5'-OH-RNA-2',3'-cyclic phosphate ligation but is able to seal a preguanylylated substrate Escherichia coli
6.5.1.8 H337A the mutant shows about 1% of 5'-OH-RNAp ligation activity compared to the wild type enzyme Escherichia coli
6.5.1.8 K299A the mutant shows about 50% of 5'-OH-RNAp ligation activity compared to the wild type enzyme Escherichia coli
6.5.1.8 N167A the mutant shows about 65% of 5'-OH-RNAp ligation activity compared to the wild type enzyme Escherichia coli
6.5.1.8 R189A the mutation slows the step of RNAppG/5'-OH RNA sealing by a factor of 200 compared to that with wild type enzyme while decreasing the rate of RNAppG formation by 3fold Escherichia coli
6.5.1.8 R341A the mutant shows about 10% of 5'-OH-RNAp ligation activity compared to the wild type enzyme Escherichia coli
6.5.1.8 R345A the mutant shows 5'-OH-RNAp ligation activity similar to the wild type enzyme Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.5.1.8 Mn2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.5.1.8 (ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O Escherichia coli
-
 (ribonucleotide)n+m + GMP + diphosphate
-
 ?
6.5.1.8 (ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + GTP Escherichia coli
-
 (ribonucleotide)n+m + GMP + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.5.1.8 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.5.1.8 nickel-agarose column chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.5.1.8 (ribonucleotide)n-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)m + GTP + H2O
-
 Escherichia coli (ribonucleotide)n+m + GMP + diphosphate
-
 ?
6.5.1.8 (ribonucleotide)n-3'-phosphate + 5'-hydroxy-(ribonucleotide)m + GTP
-
 Escherichia coli (ribonucleotide)n+m + GMP + diphosphate
-
 ?
6.5.1.8 additional information the enzyme joins RNA 2',3'-cyclic phosphate or RNA 3'-phosphate ends to 5'-OH RNA ends in a multistep pathway whereby the enzyme hydrolyzes RNA 2',3'-cyclic phosphate to RNA 3'-phosphate, transfers GMP from GTP to RNA 3'-phosphate to form to RNAppG, and directs the attack of 5'-OH on RNAppG to form a 3'-5' phosphodiester splice junction Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.5.1.8 ? x * 40000, SDS-PAGE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
6.5.1.8 rtcB
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.5.1.8 GTP
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
6.5.1.8 physiological function the enzyme operates during the unfolded protein response Escherichia coli