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Literature summary for 3.1.26.4 extracted from

  • Ratcliff, K.; Marqusee, S.
    Identification of residual structure in the unfolded state of ribonuclease H1 from the moderately thermophilic Chlorobium tepidum: comparison with thermophilic and mesophilic homologues (2010), Biochemistry, 49, 5167-5175.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of recombinant chimeric and point mutant enzymes in Escherichia coli strain BL21(DE3), I53 and L56 point mutants are expressed insolubly in inclusion bodies Chlorobaculum tepidum
expression of recombinant chimeric mutant enzyme and of His-tagged mutant L56S in Escherichia coli strain BL21(DE3) Thermus thermophilus

Protein Variants

Protein Variants Comment Organism
I53A site-directed mutagenesis Chlorobaculum tepidum
I53D site-directed mutagenesis Chlorobaculum tepidum
L56A site-directed mutagenesis Chlorobaculum tepidum
L56D site-directed mutagenesis Chlorobaculum tepidum
L56S site-directed mutagenesis Thermus thermophilus
L56S site-directed mutagenesis Chlorobaculum tepidum
additional information construction of chimeric proteins of the Thermus thermophilus enzyme with the folding core of Chlorobium tepidum RNaseH, thermal stability analysis, overview Thermus thermophilus
additional information construction of chimeric proteins of the Thermus thermophilus enzyme with the folding core of Chlorobium tepidum RNaseH, thermal stability analysis, overview Chlorobaculum tepidum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information thermodynamic analyses of chimeric proteins, overview Chlorobaculum tepidum
additional information
-
additional information thermodynamic analyses of mutant enzymes, overview Thermus thermophilus

Organism

Organism UniProt Comment Textmining
Chlorobaculum tepidum
-
-
-
Thermus thermophilus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant recombinant chimeric and point mutant enzymes from Escherichia coli strain BL21(DE3) by heparin affinity chromatography Chlorobaculum tepidum
recombinant recombinant chimeric mutant enzyme from Escherichia coli strain BL21(DE3) by heparin affinity chromatography, and His-tagged mutant L56S by nickel affinitychromatography Thermus thermophilus

Renatured (Commentary)

Renatured (Comment) Organism
recombinant I53 and L56 point mutants after being expressed insolubly in inclusion bodies in Escherichia coli Chlorobaculum tepidum

Synonyms

Synonyms Comment Organism
CtepRNH
-
Chlorobaculum tepidum
RNase H
-
Thermus thermophilus
RNase H
-
Chlorobaculum tepidum
TthRNH
-
Thermus thermophilus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
analysis of thermal unfolding, the folding core of Chlorobium tepidum RNaseH plays an important role in the unfolded state of this protein Chlorobaculum tepidum
additional information
-
analysis of thermal unfolding, the folding core of Thermus thermophilus RNaseH plays an important role in the unfolded state of this protein Thermus thermophilus