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However, none of the fungal strains, including the best mutants, are able to produce high levels of the enzymes at the same time.
Furthermore, the mutants are able to hydroxylate chrysene in different positions, producing four metabolites, 1-, 3-, 4-, and 6-hydroxychrysene, and to hydroxylate pyrene to 1-hydroxypyrene.
The TREX1 D18N and V201D mutants are able to bind both metals in the active site, but with inter-metal distances that are larger than optimal for catalysis.
Two mutants are able to switch between extracellular tachyzoites and intracellular tachyzoites but are unable to form bradyzoites.
This indicates that these mutants are able to be transported but may not stably accumulate at the poles.
It was previously reported that daf-22 mutants are able to form dauer larvae at a frequency similar to N2 at 27°C [52].
Hence, these mutants are able to abrogate the binding of NEDD1 to γ-tubulin, and therefore the centrosomal localization of γ-tubulin.
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All mutants were able to grow normally showing no difference with their respective controls.
All these mutants were able to accelerate the rate of insulin precipitation.
Unexpectedly, this latter was able to inhibit a GH11 enzyme, but not GH12, whereas the mutants were able to modulate the inhibition capacity.
Interestingly, the mutants were able to grow and to produce macedocin at considerably higher concentrations of NaCl compared to the wild-type (up to 4.0% w/v).
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