Sandbox Reserved 1565: Difference between revisions

<scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase</scene> (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>PMID: 31416831</ref>. Additional ligands of IMPDH include nicotinamide adenine dinucleotide (NAD), acetate (ACT), and 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 malignant transformation, tumor cell proliferation, and intracellular and extracellular pathogenic infections. Purine dinucleoside 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>PMID: 31416831</ref>.