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Literature summary for 3.1.26.13 extracted from

  • Lu, M.; Ngo, W.; Mei, Y.; Munshi, V.; Burlein, C.; Loughran, M.; Williams, P.; Hazuda, D.; Miller, M.; Grobler, J.; Diamond, T.; Lai, M.
    Purification of untagged HIV-1 reverse transcriptase by affinity chromatography (2010), Protein Expr. Purif., 71, 231-239.
    View publication on PubMed
Search for more literature for 3.1.26.13

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required for catalytic activity Human immunodeficiency virus 1
Mn2+ activates, required for catalytic activity Human immunodeficiency virus 1

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
-
 HIV-1
-

Purification (Commentary)

Purification (Comment) Organism
a HIV-1 RNase H specific inhibitor from the hydroxyimide class, that contains a primary amine with a long nonfunctional linker, is conjugated to NHS-activated HiTrap HP resins for use in affinity chromatographic HIV reverse transcriptase purifcation. Purification of untagged HIV-1 RT using an avidin affinity column in presence of Mg2+, method evaluations, overview Human immunodeficiency virus 1

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information RNA-DNA substrate Human immunodeficiency virus 1 ?
-
 ?

Synonyms

Synonyms Comment Organism
RNase H
-
 Human immunodeficiency virus 1

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at room temperature Human immunodeficiency virus 1

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
 assay at Human immunodeficiency virus 1

General Information

General Information Comment Organism
additional information the active site of RNase H consists of four highly conserved carboxylate residues, D443, E478, D498, and D549, and requires Mg2+ or Mn2+ for its catalytic activity Human immunodeficiency virus 1