Literature summary for 2.7.7.49 extracted from

Permanasari, E.D.; Yasukawa, K.; Kanaya, S.
Enzymatic activities of RNase H domains of HIV-1 reverse transcriptase with substrate binding domains of bacterial RNases H1 and H2 (2015), Mol. Biotechnol., 57, 526-538.

Search for more literature for 2.7.7.49

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Human immunodeficiency virus 1

Protein Variants

Protein Variants	Comment	Organism
additional information	the isolated RNase H domain of HIV-1 reverse transcriptase is inactive. Two chimeric proteins, carrying the hybrid binding domain of either Thermotoga maritima RNase H1 or Geobacillus stearothermophilus RNase H2 bind to RNA/DNA hybrids more strongly than the RNase H domain of HIV and exhibit enzymatic activity in the presence of Mn2+ ions. Activity in the presence of Mg2+ ions is very weak or absent	Human immunodeficiency virus 1

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mn2+	isolated RNase H domain, very weak activity in presence of Mn2+	Human immunodeficiency virus 1

Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	-	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)