Sandbox Reserved 1565

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== Function(s) and Biological Relevance ==
== Function(s) and Biological Relevance ==
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Inosine-5'-monophosphate dehydrogenase (IMPDH) is the enzyme that catalyzes the rate-limiting step in the ''de novo'' guanine nucleotide biosynthetic pathway, converting inosine monophosphate (IMP) to xanthosine monophosphate (XMP) with the reduction of nicotinamide adenine dinucleotide (NAD). Organisms that undergo the purine nucleotide biosynthetic pathway have IMPDH, including humans. This particular form of IMPDH described and highlighted comes from the recently studied fungus ''Ashbya gossypii'' <ref>31416831</ref>.
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Inosine-5'-monophosphate dehydrogenase (IMPDH) is the enzyme that catalyzes the rate-limiting step in the ''de novo'' guanine nucleotide biosynthetic pathway, converting inosine monophosphate (IMP) to xanthosine monophosphate (XMP) with the reduction of nicotinamide adenine dinucleotide (NAD). Organisms that undergo the purine nucleotide biosynthetic pathway have IMPDH, including humans. This particular form of IMPDH described and highlighted comes from the recently studied fungus ''Ashbya gossypii'' <ref>31416831</ref>. Additional ligands of IMPDH include nicotinamide adenine dinucleotide (NAD), acetate (ACT), guanosine-5’ monophosphate (5GP). IMPDH is a regulator of the intracellular guanine nucleotide pool amount and helps control control cell division and proliferation, and therefore related to tumor cell proliferation and intracellular and extracellular pathogenic infections. Purine dicleoside polyphosphates are found to bind to the Bateman domain of ''Ashbya gossypii'' IMPDH to allosterically regulate the catalytic activity by competing against purine mononucleotides<ref>31416831</ref>.
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== Broader Implications ==
== Broader Implications ==

Revision as of 01:28, 1 December 2019

This Sandbox is Reserved from Aug 26 through Dec 12, 2019 for use in the course CHEM 351 Biochemistry taught by Bonnie_Hall at the Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1556 through Sandbox Reserved 1575.
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Inosine-5'-monophosphate dehydrogenase

Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP

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References

1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.

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