Literature summary for 3.1.26.4 extracted from

Kanaya, S.; Nakai, C.; Konishi, A.; Inoue, H.; Ohtsuka, E.; Ikehara, M.
A hybrid ribonuclease H. A novel RNA cleaving enzyme with sequence-specific recognition (1992), J. Biol. Chem., 267, 8492-8498.

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Protein Variants

Protein Variants	Comment	Organism
additional information	a Cys residue is substituted for Glu135 by site-directed mutagenesis in the mutant enzyme, in which all 3 free Cys residues are replaced by Ala and coupled with a maleimide group which is attached to the 5'-terminus of the nonadeoxyribonucleotide, 5'-GTCATCTCC-3', with a flexible tether. The resulting hybrid enzyme d9-C135/RNase H cleaves the phosphodiester bond between the fifth and sixth residues of the complementary nonaribonucleotide without addition of the oligodeoxyribonucleotide. The nonaribonucleotide is cleaved by the wild-type or unmodified mutant enzyme only when the complemetary oligoribonucleotide is present	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
RNA-DNA hybrid + H2O	-	Escherichia coli	ribonucleotide 5'-phosphomonoester	-	?

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Release 2023.1 (January 2023)