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

BRENDA support

Literature summary for 3.1.26.12 extracted from

  • Callaghan, A.J.; Redko, Y.; Murphy, L.M.; Grossmann, J.G.; Yates, D.; Garman, E.; Ilag, L.L.; Robinson, C.V.; Symmons, M.F.; McDowall, K.J.; Luisi, B.F.
    Zn-link: a metal-sharing interface that organizes the quaternary structure and catalytic site of the endoribonuclease, RNase E (2005), Biochemistry, 44, 4667-4675.
    View publication on PubMed
Search for more literature for 3.1.26.12

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzyme and N-terminal catalytic domains in Escherichia coli Escherichia coli

Protein Variants

Protein Variants Comment Organism
C404A site-directed mutagenesis, mutation of a zinc binding residue, the mutant shows 200fold decreased activity relative to that of the wild-type enzyme for cleaving a 10-mer RNA substrate, and forms a dimer instead of a tetramer Escherichia coli
C407A site-directed mutagenesis, mutation of a zinc binding residue, the mutant shows 200fold decreased activity relative to that of the wild-type enzyme for cleaving a 10-mer RNA substrate, and forms a dimer instead of a tetramer Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Diamide treatment of the N-terminal catalytic domain with diamide causes complete loss of the zinc, but only slightly reduced activity as tetramer Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Escherichia coli
Zn2+ catalytic activity does not require zinc directly but does require the quaternary structure, for which the metal is essential, binding and coordination site structure, overview Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
124000 132000 MW of recombinant dimeric ribonuclease E N-terminal catalytic domains of mutants C404A and C407A by mass spectrometry, gel filtration, and sequence calculations, overview Escherichia coli
247500
-
 tetrameric wild-type ribonuclease E N-terminal catalytic domain, sequence calculation Escherichia coli
248800
-
 tetrameric wild-type ribonuclease E N-terminal catalytic domain, mass spectrometry Escherichia coli
270000
-
 about, tetrameric wild-type ribonuclease E N-terminal catalytic domain, gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli ribonuclease E is an essential hydrolytic endonuclease in Escherichia coli, and it plays a central role in maintaining the balance and composition of the messenger RNA population ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P21513
-
-

Purification (Commentary)

Purification (Comment) Organism
native and recombinant ribonuclease E N-terminal catalytic domains from transformed Escherichia coli Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information ribonuclease E is an essential hydrolytic endonuclease in Escherichia coli, and it plays a central role in maintaining the balance and composition of the messenger RNA population Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
dimer mutants C404A and C407A Escherichia coli
More RNase E is divided into domains of defined function and structure, the tetramer has two nonequivalent subunit interfaces, one of which is mediated by a single, tetrathiol-zinc complex, which we refer to as a Zn-link motif. One or both interfaces organize the active site, which is distinct from the primary site of RNA binding Escherichia coli
tetramer wild-type enzyme Escherichia coli

Synonyms

Synonyms Comment Organism
RNase E
-
 Escherichia coli

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Escherichia coli