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Mutagenesis of the conserved aspartic acid 443, glutamic acid 478, asparagine 494, and aspartic acid 498 residues in the ribonuclease H domain of p66/p51 human immunodeficiency virus type I reverse transcriptase. Expression and biochemical analysis.
Mizrahi V, Brooksbank RL, Nkabinde NC. Mizrahi V, et al. J Biol Chem. 1994 Jul 29;269(30):19245-9. J Biol Chem. 1994. PMID: 7518454 Free article.
The mutants fell into two classes: (i) functional RT, but not detectable ribonuclease H activity, and (ii) uncharacterizable phenotype due to protein instability in the context of the RT/protease Escherichia coli co-expression system (Mizrahi, V., Lazarus, G. M., Mi …
The mutants fell into two classes: (i) functional RT, but not detectable ribonuclease H activity, and (ii) uncharacterizable phenotype due t …
Kinetic mechanism of DNA polymerase I (Klenow).
Kuchta RD, Mizrahi V, Benkovic PA, Johnson KA, Benkovic SJ. Kuchta RD, et al. Among authors: mizrahi v. Biochemistry. 1987 Dec 15;26(25):8410-7. doi: 10.1021/bi00399a057. Biochemistry. 1987. PMID: 3327522
The rate is not limited by the actual polymerization but by a separate step, possibly important in ensuring fidelity [Mizrahi, V., Henrie, R. N., Marlier, J. F., Johnson, K. A., & Benkovic, S. J. (1985) Biochemistry 24, 4010-4018]. ...
The rate is not limited by the actual polymerization but by a separate step, possibly important in ensuring fidelity [Mizrahi, V
176 results