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Literature summary for 3.1.26.12 extracted from

  • Diwa, A.A.; Jiang, X.; Schapira, M.; Belasco, J.G.
    Two distinct regions on the surface of an RNA-binding domain are crucial for RNase E function (2002), Mol. Microbiol., 46, 959-969.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes Escherichia coli

Protein Variants

Protein Variants Comment Organism
F57A site-directed mutagenesis, 91% reduced feedback regulation activity compared to the wild-type enzyme Escherichia coli
F67A site-directed mutagenesis, 94% reduced feedback regulation activity compared to the wild-type enzyme Escherichia coli
K106A site-directed mutagenesis, 60% reduced feedback regulation activity compared to the wild-type enzyme Escherichia coli
K112A site-directed mutagenesis, 94% reduced feedback regulation activity compared to the wild-type enzyme Escherichia coli
K37A site-directed mutagenesis, 94% reduced feedback regulation activity compared to the wild-type enzyme Escherichia coli
K38A site-directed mutagenesis, 49% reduced feedback regulation activity compared to the wild-type enzyme Escherichia coli
K43A site-directed mutagenesis, 33% reduced feedback regulation activity compared to the wild-type enzyme Escherichia coli
K71A site-directed mutagenesis, 56% reduced feedback regulation activity compared to the wild-type enzyme Escherichia coli
R109A site-directed mutagenesis, 78% reduced feedback regulation activity compared to the wild-type enzyme Escherichia coli
R48A site-directed mutagenesis, 49% reduced feedback regulation activity compared to the wild-type enzyme Escherichia coli
R64A site-directed mutagenesis, 77% reduced feedback regulation activity compared to the wild-type enzyme Escherichia coli
R87A site-directed mutagenesis, 16% increased feedback regulation activity compared to the wild-type enzyme Escherichia coli
R95A site-directed mutagenesis, 19% increased feedback regulation activity compared to the wild-type enzyme Escherichia coli
Y42A site-directed mutagenesis, 48% reduced feedback regulation activity compared to the wild-type enzyme Escherichia coli
Y60A site-directed mutagenesis, 99% reduced feedback regulation activity compared to the wild-type enzyme Escherichia coli
Y77A site-directed mutagenesis, 19% reduced feedback regulation activity compared to the wild-type enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli the enzyme, especially its catalytic N-terminal domain, is essential for RNA processing and degradation, and for cell growth and feedback regulation of RNase E synthesis ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes, purification involves denaturation and renaturation steps due to the poor solubility of the full-length enzyme Escherichia coli

Renatured (Commentary)

Renatured (Comment) Organism
recombinant wild-type and mutant enzymes, purification involves denaturation and renaturation steps due to the poor solubility of the full-length enzyme Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
feedback regulation activity of wild-type and mutant enzymes, overview Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information reaction mechanism Escherichia coli ?
-
?
additional information the enzyme, especially its catalytic N-terminal domain, is essential for RNA processing and degradation, and for cell growth and feedback regulation of RNase E synthesis Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
More three-dimensional enzyme structure with an essential N-terminal RNase E domain of the S1 family RNA-binding domain fold, the residues involved in cell growth and feedback regulation of RNase E synthesis form two cluster, e.g. Phe57, Phe67, and Tyr112, or Lys37 and Tyr60, overview, structural modeling of the S1 domain Escherichia coli

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the S1 family of RNA-binding enzymes Escherichia coli
RNase E
-
Escherichia coli