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Literature summary for 3.6.4.13 extracted from

  • Worrall, J.A.; Howe, F.S.; McKay, A.R.; Robinson, C.V.; Luisi, B.F.
    Allosteric activation of the ATPase activity of the Escherichia coli RhlB RNA helicase (2008), J. Biol. Chem., 283, 5567-5576.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
RNase E is required for ATPase and RNA unwinding activities of the enzyme, forms a complex with the enzyme, interaction analysis, overview. Avid, enthalpy-favored interaction between the helicase and RNase E 696-762 with an equilibrium binding constant Kaof at least 1 x 108 M-1 determined by isothermal titration calorimetry. Protein-protein and RNA-binding surfaces both communicate allosterically with the ATPase catalytic center Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
construction of a di-cistronic vector that overexpresses a complex comprising RhlB and its recognition site within RNase E, corresponding to residues 696-762, the expression construct is termed pRneRhlBDELTA1-397. Expression of His-tagged wild-type and mutant RhlB and RNaseE in Escherichia coli strain BL21(DE3) Escherichia coli

Protein Variants

Protein Variants Comment Organism
D310H site-directed mutagenesis of the V motif, leads to altered enzyme activity, overview Escherichia coli
D313H site-directed mutagenesis of the V motif, leads to altered enzyme activity, overview Escherichia coli
H320D site-directed mutagenesis of the V motif, leads to altered enzyme activity, overview Escherichia coli
Y383A site-directed mutagenesis, the mutation causes the formation of a higher order molecular weight species in binding of RNaseE by RhlB Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Escherichia coli
-
ADP + phosphate
-
?
additional information Escherichia coli helicase B, RhlB, is one of the five DEAD box RNA-dependent ATPases in Escherichia coli. ATPases found in Escherichia coli. RhlB requires an interaction with the partner protein RNase E for appreciable ATPase and RNA unwinding activities ?
-
?
RNA + H2O Escherichia coli helicase/unwinding activity ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant RhlB and RNaseE from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.00000001
-
about, wild-type enzyme, RNA helicase activity Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
Escherichia coli ADP + phosphate
-
?
additional information helicase B, RhlB, is one of the five DEAD box RNA-dependent ATPases in Escherichia coli. ATPases found in Escherichia coli. RhlB requires an interaction with the partner protein RNase E for appreciable ATPase and RNA unwinding activities Escherichia coli ?
-
?
additional information RhlB is the only Escherichia coli DEAD box protein that requires a protein partner to stimulate its ATPase activity Escherichia coli ?
-
?
RNA + H2O helicase/unwinding activity Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
More location of the nine conserved sequence motifs in the DEAD box helicase RhlB, structure modelling, overview Escherichia coli

Synonyms

Synonyms Comment Organism
helicase B
-
Escherichia coli
RhlB
-
Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Escherichia coli