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Function(s) and Biological Relevance

IMP (Inosin-5’-monophosphate) dehydrogenase is an enzyme that catalyzes rate limiting step in the de novo guanine nucleotide biosynthetic pathway. It comes from a fungus known as Ashbya gossip and it is particularly interesting because of the major affect cations, like potassium have on it. IMPDH facilitates these conformational changes. It represents a therapeutic mechanism for managing several diseases including microbial infections and cancer. Furthermore, dinucleotide polyphosphates play important physiological roles in the allosteric regulation, which may have important implications for the design of therapeutic strategies to inhibit IMPDH’s as well.

Broader Implications

Dinucleoside polyphosphates have been found to participate in many different cellular processes such as DNA replication and repair, cell division, neurotransmission, apoptosis, vasoconstriction, and platelet aggregation. In a recent study done by Lizbeth Hedstrom, she mentioned how "pacemaker" enzymes, such as IMPDH are linked to neoplastic transformation and progression. Researchers discovered that if there were a way for these enzymes to become inhibited, then the growth of the tumors could be regulated and the rate of being metastasized could be controlled.

Structural highlights and structure-function relationships

Energy Transformation

As IMPDH has three nucleotide-binding sites, which aid in modulating and regulating catalytic activity, there is a large increase in affinity in this molecule. This more than likely comes from the simultaneous reduction of the entropic penalty of binding due to molecularity change.

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