Literature summary for 3.1.13.2 extracted from

Zhan, X.; Tan, C.K.; Scott, W.A.; Mian, A.M.; Downey, K.M.; So, A.G.
Catalytically distinct conformations of the ribonuclease H of HIV-1 reverse transcriptase by substrate cleavage patterns and inhibition by azidothymidylate and N-ethylmaleimide (1994), Biochemistry, 33, 1366-1372.

Search for more literature for 3.1.13.2

Inhibitors

Inhibitors	Comment	Organism	Structure
3'-azido-3'-deoxythymidine 5'-phosphate	more sensitive to inhibition with poly(rGdC) than with poly(rAdT) as substrate. Competitive inhibitor with respect to substrate in Mn2+, uncompetitive inhibitor in Mg2+	Human immunodeficiency virus 1

Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	in Mg2+, hydrolysis of poly(rAdT) appears to be solely endonucleolytic. In Mn2+, hydrolysis of poly(rAdT) is both endonucleolytic and exonucleolytic. With poly(rGdC) as substrate, hydrolysis is both endonucleolytic and exonucleolytic in either Mg2+ or Mn2+	Human immunodeficiency virus 1	?	-	?
RNA-DNA hybrid + H2O	poly(rGdC)	Human immunodeficiency virus 1	ribonucleotide 5'-phosphomonoester	-	?

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)