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The dramatic stimulation of enzyme activity by azide and fluoride restores activity in otherwise marginally active D32A variants to near wild-type levels, suggesting that these anions functionally replace the Asp 32 carboxylate.
However, the addition of Mg2+ restores activity.
Correcting the misrouting of misfolded mutant proteins often restores activity and addresses the underlying disease.
These screens identified a glycine to serine mutation of L30e, which specifically restores activity to an RNA variant containing a U that replaces a helix-capping G. Similarly, an asparagine to alanine mutation was found to suppress a substitution at a position where the L30e RNA nucleotide extends out into the protein pocket.
Reduction of this disulfide bond by beta-mercaptoethanol restores activity, indicating that mobility of the head domain of ISP is functionally important in the cytochrome bc(1) complex.
Increasing the concentration of R102A P450cin 10-fold restores activity to only ∼18% of that of the wild type, with a kcat value of 154.4 ± 12.8 min–12.8
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Back-mutation of these residues to the consensus found in an active PTP domain was sufficient to restore activity [ 14].
These mutants are predicted to restore activity in the H266 variant (Table 1, "restorative" mutants; Figure 2b).
The hybrids were however not as active as the parent GAEL 1 against MiaPaCa2 whereas 6 restored activity comparable to 1.
Neuronal homeostatic synaptic scaling then provides a feedback mechanism to restore activity.
Tryptophanamides with aliphatic side chains were inactive whereas basic residues restored activity.
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