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Here, we describe the role of Asp121 in modulating the enzyme's pH-activity profile.
On the other hand, the differential role of the two subunits of PFK could also be due to the differences in their associations with the cAMP pathway, which as this study shows is responsible for modulating the enzyme activities of the glycolytic enzymes in such a way that the system becomes unstable and starts to oscillate.
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Structural and kinetic characterizations of an evolved SULT variant show how few ancestral mutations reshaped the active site and modulated the enzyme's specificity.
Altering the length of the repeat region could then alter the interactions between the conserved N- and C-terminal domains, and so modulate the enzyme's catalytic properties, in particular its substrate specificity.
Cross-talk between the catalytic core and the C-terminal regulatory domain modulates the enzyme activity.
This is also the case for the regulatory site in which ADP binds to allosterically modulate the enzyme.
In several enzyme families, changes in the domain alliances are known to modulate the enzyme function, usually by altering the substrate specificity or enzyme efficiency.
It is plausible that the mutation modulates the enzyme's translocation kinetics by altering the rates of transition between these two conformations.
Conformational changes in Ire1's kinase domain modulate the enzyme's predisposition to form oligomers, in which Ire1-Ire1 contacrosscross multiple interfaces activate Ire1's RNase activity.
In both orders, selection also targeted an α-helix/loop element in RNase L that modulates the enzyme preference for single-stranded RNA versus stem loops.
A recent study has given new insights into the molecular arrangement of RuvBL1 and RuvBL2 and strongly suggested that in vivo activities are regulated by cofactors inducing conformational changes via domain II in order to modulate the enzyme complex into its active state.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com