Naively, one expects the information communicated by an enzyme downstream within a signaling network, in which the enzyme is embedded, to grow monotonically with the enzyme's rate of product formation. However, here we observe that this does not necessarily hold true for allosterically regulated enzymes, often observed in signaling networks. In particular, we find that the mutual information between the catalytic sites of an allosterically regulated enzyme and a receiver protein downstream in the signaling pathway depends on the transition kinetics between the different allosterically regulated states of the enzyme and their respective rates of product formation. Surprisingly, our work implies that allosteric down-regulation of an enzyme's rate of product formation may not only be used as a way to silence itself, as one would normally expect. Rather, down-regulation may also be used to increase the information communicated by this enzyme to a receiver protein downstream in a signaling pathway.
ASJC Scopus subject areas
- Physics and Astronomy(all)