Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Walsh, A.P.; Tock, M.R.; Mallen, M.H.; Kaberdin, V.R.; von Gabain, A.; McDowall, K.J.
    Cleavage of poly(A) tails on the 3'-end of RNA by ribonuclease E of Escherichia coli (2001), Nucleic Acids Res., 29, 1864-1871.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.26.12 expression of His-tagged full-length wild-type RNase E and His-tagged N-terminal ribonucleolytic domain RTD-RNase E, residues 1-498, in strain BL21(DE3) Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.26.12 additional information the enzyme is not inhibitable by commercially available RNase A inhibitor Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.26.12 additional information the enzyme is part of the RNA degradosome multi-protein complex, which also contains enolase, RhlB, and PNPase Escherichia coli
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.26.12 Mg2+
-
 Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.1.26.12 Escherichia coli
-
-
-
3.1.26.12 Escherichia coli BRL2288
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.26.12 native RNA degradosome from strain BRL2288, recombinant His-tagged full-length wild-type RNase E and His-tagged N-terminal ribonucleolytic domain RTD-RNase E from strain BL21(DE3) by metal affinity chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.26.12 RNA + H2O the enzyme or its isolated N-terminal catalytic domain cleave poly(A) tails on the 3' end of RNA substrates, the RNA degradosome cleaves 3' poly(A) tails of RNA irrespective of the 5' phosphorylation status, while the purified RNase E shows high preference for 5'-monophosphorylated RNA substrates, and low activity with 5'-triphosphate RNA, N-terminal ribonucleolytic domain RTD-RNase E is the catalytic domain and sufficient for activity Escherichia coli ?
-
 ?
3.1.26.12 RNA + H2O the enzyme or its isolated N-terminal catalytic domain cleave poly(A) tails on the 3' end of RNA substrates, the RNA degradosome cleaves 3' poly(A) tails of RNA irrespective of the 5' phosphorylation status, while the purified RNase E shows high preference for 5'-monophosphorylated RNA substrates, and low activity with 5'-triphosphate RNA, N-terminal ribonucleolytic domain RTD-RNase E is the catalytic domain and sufficient for activity Escherichia coli BRL2288 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.26.12 More N-terminal ribonucleolytic domain RTD-RNase E is the catalytic domain and sufficient for activity Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.1.26.12 ribonuclease E
-
 Escherichia coli
3.1.26.12 RNase E
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.26.12 37
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.26.12 7.6
-
 assay at Escherichia coli