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Literature summary for 3.1.26.12 extracted from

  • Bandyra, K.J.; Wandzik, J.M.; Luisi, B.F.
    Substrate recognition and autoinhibition in the central ribonuclease RNase E (2018), Mol. Cell, 72, 275-285.e4 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of RNase E in complex with the sRNA RprA reveals a duplex recognition site that saddles an inter-protomer surface to help present substrates for cleavage Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
RNA + H2O Escherichia coli
-
?
-
?
RNA + H2O Escherichia coli K12
-
?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P21513
-
-
Escherichia coli K12 P21513
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
RNA + H2O
-
Escherichia coli ?
-
?
RNA + H2O RNase E recognizes RNA secondary structure. Signature on the substrate 50 end recognizes and activates RNase E Escherichia coli ?
-
?
RNA + H2O
-
Escherichia coli K12 ?
-
?
RNA + H2O RNase E recognizes RNA secondary structure. Signature on the substrate 50 end recognizes and activates RNase E Escherichia coli K12 ?
-
?

Synonyms

Synonyms Comment Organism
RNase E
-
Escherichia coli

General Information

General Information Comment Organism
physiological function RNase E is a central ribonuclease of RNA metabolism and post-transcriptional control of gene expression Escherichia coli