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Literature summary for 6.5.1.8 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
Search for more literature for 6.5.1.8

Protein Variants

Protein Variants Comment Organism
C78A completely inactive Escherichia coli
D75A the mutation allows cyclic phosphodiester hydrolysis but cripples 3'-phosphate guanylylation Escherichia coli
H168A the mutant shows about 48% of 5'-OH-RNAp ligation activity compared to the wild type enzyme Escherichia coli
H185A the mutant shows 5'-OH-RNAp ligation activity similar to the wild type enzyme Escherichia coli
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
H337A the mutant shows about 1% of 5'-OH-RNAp ligation activity compared to the wild type enzyme Escherichia coli
K299A the mutant shows about 50% of 5'-OH-RNAp ligation activity compared to the wild type enzyme Escherichia coli
N167A the mutant shows about 65% of 5'-OH-RNAp ligation activity compared to the wild type enzyme Escherichia coli
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
R341A the mutant shows about 10% of 5'-OH-RNAp ligation activity compared to the wild type enzyme Escherichia coli
R345A the mutant shows 5'-OH-RNAp ligation activity similar to the wild type enzyme Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

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

Synonyms

Synonyms Comment Organism
rtcB
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
GTP
-
 Escherichia coli

General Information

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