Literature summary for 3.1.26.13 extracted from

Rausch, J.W.; Lener, D.; Miller, J.T.; Julias, J.G.; Hughes, S.H.; Le Grice, S.F.J.
Altering the RNase H primer grip of human immunodeficiency virus reverse transcriptase modifies cleavage specificity (2002), Biochemistry, 41, 4856-4865.

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Protein Variants

Protein Variants	Comment	Organism
E475A	site-directed mutagenesis, the mutant shows only minimally altered substrate specificity or enzyme activity compared to the wild-type enzyme. But the efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera	Human immunodeficiency virus 1
I505G	site-directed mutagenesis, the mutant exhibits a dimerization defect. The efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera	Human immunodeficiency virus 1
K476A	site-directed mutagenesis, the mutant shows only minimally altered substrate specificity or enzyme activity compared to the wild-type enzyme. But the efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera	Human immunodeficiency virus 1
additional information	RNase H primer grip mutations suppress polymerization-independent RNase H cleavage. Alteration of RNase H primer grip residues Thr473, Asn474, and Gln475 has little influence on cleavage specificity. Altering the RNase H domain of HIV-1 RT can impact significantly on the ability of mutant enzymes to catalyze DNA synthesis, but all RNase H primer grip mutants show little difference in their DNA-dependent DNA polymerase activity	Human immunodeficiency virus 1
T473A	site-directed mutagenesis, the mutant shows only minimally altered substrate specificity or enzyme activity compared to the wild-type enzyme. But the efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera	Human immunodeficiency virus 1
Y501A	site-directed mutagenesis, the mutant shows only minimally altered substrate specificity or enzyme activity compared to the wild-type enzyme. But the efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera	Human immunodeficiency virus 1

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Human immunodeficiency virus 1

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Human immunodeficiency virus 1	conserved residues in the connection subdomain and C-terminal ribonuclease H, RNase H, domain of HIV-1 RT contact the nascent DNA primer and modulate the trajectory of the template relative to the RNase H catalytic center. Within the RNase H domain, these residues include Thr473, Glu475, Lys476, Tyr501, and Ile505, while His539 and Asn474 interact with the scissile phosphate of the RNA template,m substrate recognition and binding, overview	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	-	HIV-1	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	conserved residues in the connection subdomain and C-terminal ribonuclease H, RNase H, domain of HIV-1 RT contact the nascent DNA primer and modulate the trajectory of the template relative to the RNase H catalytic center. Within the RNase H domain, these residues include Thr473, Glu475, Lys476, Tyr501, and Ile505, while His539 and Asn474 interact with the scissile phosphate of the RNA template,m substrate recognition and binding, overview	Human immunodeficiency virus 1	?	-	?

Subunits

Subunits	Comment	Organism
dimer	HIV-1 RT	Human immunodeficiency virus 1

Synonyms

Synonyms	Comment	Organism
human immunodeficiency virus reverse transcriptase	-	Human immunodeficiency virus 1
RNase H	-	Human immunodeficiency virus 1

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Human immunodeficiency virus 1

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Human immunodeficiency virus 1

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Release 2023.1 (January 2023)