Literature summary for 2.7.7.49 extracted from

Herman, B.D.; Sluis-Cremer, N.
Transient kinetic analyses of the ribonuclease H cleavage activity of HIV-1 reverse transcriptase in complex with efavirenz and/or a beta-thujaplicinol analogue (2013), Biochem. J., 455, 179-184.

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Inhibitors

Inhibitors	Comment	Organism	Structure
2,7-dihydroxy-2,4,6-cyclo-heptatrien-1-one	beta-thujaplicinol analogue. Compound has no effect on polymerase-dependent RNase H cleavages but significantly affects the rates of polymerase-independent RNase H cleavages. In a model, the compoouind binds to the RNase H active site after the primary polymerase-dependent RNase H cleavage has occurred and stabilizes the 3'-end of the DNA primer in the polymerase active site thus blocking the enzyme's ability to carry out the polymerase-independent cleavages	Human immunodeficiency virus 1
efavirenz	Compound has no effect on polymerase-dependent RNase H cleavages but significantly affects the rates of polymerase-independent RNase H cleavages. Efavirenz destabilizes the 3'-end of the DNA primer in the DNA polymerase active site and promotes RT-mediated polymerase-independent cleavages	Human immunodeficiency virus 1

Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	-	-	-

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Release 2023.1 (January 2023)