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

BRENDA support

Literature summary for 3.1.26.13 extracted from

  • Oda, M.; Xi, Z.; Inaba, S.; Slack, R.; Ishima, R.
    Binding thermodynamics of metal ions to HIV-1 ribonuclease H domain (2019), J. Therm. Anal. Calorim., 135, 2647-2653 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.26.13

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information analysis of the binding thermodynamics and structural effect of divalent metal ions, i.e. Mn2+, Zn2+, and Mg2+, to the isolated ribonuclease H (RNH) of human immunodeficiency virus (HIV) using isothermal titration calorimetry and circular dichroism, overview Human immunodeficiency virus type 1 group M subtype B

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ binding thermodynamics of Mg2+ to RNH, Mg2+ binding has little effect on the thermal stability of enzyme domain RNH Human immunodeficiency virus type 1 group M subtype B
Mn2+ Mn2+ binding increased the stability of the enzyme domain RNH Human immunodeficiency virus type 1 group M subtype B
additional information structural effect of divalent metal ions, i.e. Mn2+, Zn2+, and Mg2+, to the isolated ribonuclease H (RNH) of human immunodeficiency virus (HIV) using isothermal titration calorimetry and circular dichroism, overview. The binding affinity of Mg2+ is about 40 and 400 times lower than those of Mn2+ and of Zn2+, respectively. The structural analysis shows that Mg2+ binding has little effect on the thermal stability of RNH, while Zn2+ and Mn2+ binding increased the stability Human immunodeficiency virus type 1 group M subtype B
Zn2+ Zn2+ binding increased the stability of the enzyme domain RNH Human immunodeficiency virus type 1 group M subtype B

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus type 1 group M subtype B
-
 HIV-1
-
Human immunodeficiency virus type 1 group M subtype B BH10
-
 HIV-1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information usage of DNA/RNA hybrid substrates for enzyme activity assay. The isolated RNH domain of reverse transcriptase (RT), folded by itself, is not catalytically active, due to lack of the substrate handle region, but exhibits a native-like protein fold Human immunodeficiency virus type 1 group M subtype B ?
-
 ?
additional information usage of DNA/RNA hybrid substrates for enzyme activity assay. The isolated RNH domain of reverse transcriptase (RT), folded by itself, is not catalytically active, due to lack of the substrate handle region, but exhibits a native-like protein fold Human immunodeficiency virus type 1 group M subtype B BH10 ?
-
 ?

Synonyms

Synonyms Comment Organism
HIV-1 ribonuclease H domain
-
 Human immunodeficiency virus type 1 group M subtype B
RNH
-
 Human immunodeficiency virus type 1 group M subtype B

General Information

General Information Comment Organism
additional information enzyme domain RNH structure-function relationship analysis, overview Human immunodeficiency virus type 1 group M subtype B