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Literature summary for 3.1.26.12 extracted from

  • Thompson, K.; Zong, J.; Mackie, G.
    Altering the divalent metal ion preference of RNase E (2015), J. Bacteriol., 197, 477-482 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.26.12

Protein Variants

Protein Variants Comment Organism
D303C mutation results in nearly full loss of activity regardless of metal ion Escherichia coli
D346C the mutation leads to almost complete loss of activity dependent on Mg2+. The activity of the mutant enzyme is fully restored by the presence of Mn2+ with kinetic parameters fully equivalent to those of wild-type enzyme Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
intracellular
-
 Escherichia coli 5622
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ RNase E requires a divalent metal ion for its activity. Mg2+ is the physiological divalent metal ion supporting activity of RNase E in vivo. Mg2+ and Mn2+ support significant rates of activity in vitro against natural RNAs, with Mn2+ being preferred. Both Mg2+ and Mn2+ also support cleavage of an oligonucleotide substrate with similar kinetic parameters for both ions Escherichia coli
Mn2+ RNase E requires a divalent metal ion for its activity. Mg2+ is the physiological divalent metal ion supporting activity of RNase E in vivo. Mg2+ and Mn2+ support significant rates of activity in vitro against natural RNAs, with Mn2+ being preferred. Both Mg2+ and Mn2+ also support cleavage of an oligonucleotide+substrate with similar kinetic parameters for both ions Escherichia coli
additional information Ca2+, Co3+, Cu2+ and Fe2+ are unable to support the activity of RNase E Escherichia coli
Ni2+ RNase E requires a divalent metal ion for its activity. Mg2+ is the physiological divalent metal ion supporting activity of RNase E in vivo. Ni2+ and Zn2+ permits low levels of activity in vitro Escherichia coli
Zn2+ RNase E requires a divalent metal ion for its activity. Mg2+ is the physiological divalent metal ion supporting activity of RNase E in vivo. Ni2+ and Zn2+ permits low levels of activity in vitro Escherichia coli

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.
5'P-BR14FD + H2O synthetic RNA substrate 5'P-BR14FD Escherichia coli ?
-
 ?
5'P-BR14FD + H2O synthetic RNA substrate 5'P-BR14FD Escherichia coli K12 ?
-
 ?

Synonyms

Synonyms Comment Organism
RNase E
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function the enzyme participates in most aspects of RNA processing and degradation Escherichia coli