Literature summary for 3.1.26.13 extracted from

Misra, H.; Pandey, P.; Pandey, V.
An enzymatically active chimeric HIV-1 reverse transcriptase (RT) with the RNase-H domain of murine leukemia virus RT exists as a monomer (1998), J. Biol. Chem., 273, 9785-9789.

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Protein Variants

Protein Variants	Comment	Organism
additional information	construction of a chimeric enzyme containing the first 425 amino acid residues from the N-terminal domain of HIV-1 reverse transcriptase, i.e. the polymerase domain, and 200 amino acid residues from the C-terminal domain of murine leukemia virus reverse transcriptase, i.e. RNase H-domain. The chimeric enzyme exists as a monomer with intact DNA polymerase and RNase-H functions. It is able to catalyze both endonucleolytic and processive RNase-H functions in a manner similar to the wild type HIV-1 reverse transcriptase and murineleukemia virus reverse transcriptase	murine leukemia virus

Organism

Organism	UniProt	Comment	Textmining
murine leukemia virus	-	-	-

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Release 2023.1 (January 2023)