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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. IMP dehydrogenase helps make it easier to make a purine, without it, it is very complicated. Here shows a view of the labeled in light pink. (Fernandez-Justel, David, et al. pg. 14768).

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. (Fernandez-Justel, David, et al. pg. 14768).

Structural highlights and structure-function relationships

showing the N terminus in blue and C terminus in red. The active sites are located near the C terminus. The catalytic domain of this protein is where the ligands, active sites, and the catalytic triad is located.

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

This shows view. The space filling view helps display van der waals interactions which is important to visualize on a protein. This view shows the molecules in purple.

This view shows the parts in yellow. The negative area shows the phosphate backbone as well.

This view shows the in the protein.

This view shows the areas. (Fernandez-Justel, David, et al. pg. 14768-14771). labeled in purple dots.

Energy Transformation

The Bateman domain of eukaryotic IMPDH's has three nucleotide-binding sites that operate coordinately to allosterically modulate the catalytic activity. View. Dinucleoside polyphosphates modulate the catalytic activity of IMPDHs in vitro by efficiently competing with the adenine/guanine mono nucleotides for the allosteric sites. (Fernandez-Justel, David, et al. pg. 14768).