Literature summary for 3.1.26.13 extracted from

Lener, D.; Budihas, S.R.; Le Grice, S.F.J.
Mutating conserved residues in the ribonuclease H domain of Ty3 reverse transcriptase affects specialized cleavage events (2002), J. Biol. Chem., 277, 26486-26495.

Search for more literature for 3.1.26.13

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
D358N	mutation eliminates Mg2+- and Mn2+-dependent RNase H function	Saccharomyces cerevisiae
D426N	mutation eliminates Mg2+- and Mn2+-dependent RNase H function	Saccharomyces cerevisiae
D469N	reduced RNase H activity in presence of Mg2+, decrease of turnover rate in presence of Mn2+. Mutant fails to support DNA strand transfer and release of the (+)-strand polypurine tract primer from (+)-RNA	Saccharomyces cerevisiae
E401Q	mutation eliminates Mg2+- and Mn2+-dependent RNase H function	Saccharomyces cerevisiae
H427A	reduced RNase H activity in presence of Mg2+, decrease of turnover rate in presence of Mn2+. Mutant fails to support DNA strand transfer and release of the (+)-strand polypurine tract primer from (+)-RNA	Saccharomyces cerevisiae
Y459A	reduced RNase H activity in presence of Mg2+, decrease of turnover rate in presence of Mn2+. Mutant fails to support DNA strand transfer and release of the (+)-strand polypurine tract primer from (+)-RNA	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	retrotransposon Ty3, gypsy-group	-

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)