Sandbox Reserved 1571

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== '''Function(s) and Biological Relevance''' ==
== '''Function(s) and Biological Relevance''' ==
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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 (Fernández-Justel, et al. pg 14768). 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 (Hedstrom, n.p.).
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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 <ref>PMID: 31416831</ref/. 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 (Hedstrom, n.p.).
== '''Broader Implications''' ==
== '''Broader Implications''' ==
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== '''References''' ==
== '''References''' ==
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<ref>“5tc3.” 5tc3 - Proteopedia, Life in 3D, proteopedia.org/wiki/index.php/5tc3.</ref>
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“5tc3.” 5tc3 - Proteopedia, Life in 3D, proteopedia.org/wiki/index.php/5tc3.
Fernández-Justel, David, et al. “The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates.” Journal of Biological Chemistry, vol. 294, no. 40, 2019, pp. 14768–14775., doi:10.1074/jbc.ac119.010055.
Fernández-Justel, David, et al. “The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates.” Journal of Biological Chemistry, vol. 294, no. 40, 2019, pp. 14768–14775., doi:10.1074/jbc.ac119.010055.

Revision as of 02:21, 9 December 2019

Structure

Here you can see the structure of the protein IMP Dehydrogenase.

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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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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 [1]

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