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Once the mutant enzyme is neutralized, the healthy one puts the cell back on track.
The mutant enzyme is still catalytically competent and retains its binding with the FAD coenzyme.
However, the mutant enzyme is not necessary stable enough to use for a long term and under various conditions.
The mutant enzyme is potentially useful for the production of D-amino acids via the reductive amination of the corresponding 2-oxo acid with ammonia.
The kpyro of the mutant enzyme is ∼320 fold slower than that of the WT.
The catalytic activity of the mutant enzyme is decreased three fold when compared to the wild type RNase L, and it is no longer capable of inducing apoptosis [13].
Similar(40)
Secondary structure of the mutant enzyme was similar to the wild type enzyme.
The Leu71Ile mutant enzyme was used to assemble a cuvette-based biosensor specific for l-Asn.
The activity toward CA of the M57L mutant enzyme was too low to evaluate the effect of L-cysteine.
K m value for purified mutant enzyme was 1.8 mm with optimum pH 8.5 and temperature of 60 °C (Bokhari et al. 2010).
Fluorescence spectroscopy results demonstrated that the tertiary structure of the mutant enzyme was more compact than that of the wild-type (WT) enzyme.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com