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Function(s) and Biological Relevance

IMP dehydrogenase is an enzyme that catalyzes the rate limiting de novo guanine nucleotide biosynthetic pathway. This protein comes from a fungus known as Ashbya gossypii. The pathway represents a therapeutic for managing several diseases, including microbial infections and cancer. . Dinucleoside polyphosphates play important physiological roles in the allosteric regulation of IMPDHs and may have important implications for the design of therapeutic strategies to inhibit IMPDHs.

Broader Implications

Dinucleoside polyphosphates have been described to play a part in increasing variety of cellular processes like DNA replication and repair, cell division, nuerotransmission, apoptosis, analgesia, vasoconstriction, and platlet aggregation. As it is described to play a part in these cellular processes, there is also others not mentioned it is known to play a role in. Dinucleoside polyphosphates have been described to interact with several target protiens including adenylate kinase, purinergic receptors, heat shock protiens, and poly(A) polymerase among others.

Structural highlights and structure-function relationships

This view shows the of the protein. The protein hydrophobicity can determine how it interacts with other molecules or proteins. This shows view. This view shows the molecules in purple. This view shows the parts in yellow.

Energy Transformation

The Bateman domain of eukaryotic IMPDH's has three nucleotide-binding sites that operate coordinately to allosterically modulate the catalytic activity.