Naively, one expects the Shannon information communicated by a protein downstream to a signaling network, in which the protein is embedded, to grow monotonically with this protein 's rate of product formation. Here we observe that this does not hold for allosterically regulated proteins often found in signaling networks. In particular, we find that the Shannon information communicated by an allosterically regulated protein is a complex function of the transition kinetics between its different allosterically regulated states  and their respective product formation rates . Surprisingly, our work implies that allosteric down-regulation of protein product formation may not only be used to silence proteins as one would normally expect. Rather, down-regulation may  be used to increase the Shannon information communicated by this protein in a signaling pathway.
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.
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