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Literature summary for 2.7.7.49 extracted from

  • Kerr, S.G.; Anderson, K.S.
    Pre-steady-state kinetic characterization of wild type and 3'-azido-3'-deoxythymidine (AZT) resistant human immunodeficiency virus type 1 reverse transcriptase: implication of RNA directed DNA polymerization in the mechanism of AZT resistance (1997), Biochemistry, 36, 14064-14070.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D67N/K70R/T215Y/K219Q mutation results in a 1.5fold decrease in the rate constant for polymerization and a 2.5fold decrease in the equilibrium dissociation constant for 3'-azido-3'-deoxythymidine 5'-triphosphate compared to wild-type enzyme. These values translate into a 4fold decrease in selectivity for 3'-azido-3'-deoxythymidine 5'-monophosphate incorporation ba the mutant enzyme as compared to wild-type enzyme for RNA dependent DNA replication. No such decrease in selectivity is detected for DNA dependent replication Human immunodeficiency virus 1

Organism

Organism UniProt Comment Textmining
Avian myeloblastosis virus
-
wild-type and 3'-azido-3'-deoxythymidine resistant strain D67N/K70R/T215Y/K219Q
-
Human immunodeficiency virus 1
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and 3'-azido-3'-deoxythymidine resistant strain D67N/K70R/T215Y/K219Q, expression in Escherichia coli Human immunodeficiency virus 1

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deoxynucleoside triphosphate + DNAn
-
Avian myeloblastosis virus diphosphate + DNAn+1
-
?
deoxynucleoside triphosphate + DNAn
-
Human immunodeficiency virus 1 diphosphate + DNAn+1
-
?