Sandbox Reserved 1571
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| - | ==Structure== | ||
| - | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
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| - | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
== Function(s) and Biological Relevance == | == Function(s) and Biological Relevance == | ||
Revision as of 16:24, 26 November 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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Contents |
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. 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.
Broader Implications
Dinucleoside polyphosphates have been found to participate in many different cellular processes such as DNA replication and repair, cell division, neurotransmission, apoptosis, vasoconstriction, and platelet aggregation. In a recent study done by Lizbeth Hedstrom, she mentioned how "pacemaker" enzymes, such as IMPDH are linked to neoplastic transformation and progression. Researchers discovered that if there were a way for these enzymes to become inhibited, then the growth of the tumors could be regulated and the rate of being metastasized could be controlled.
Structural highlights and structure-function relationships
In this section you will find the different views for . First, a . Also, the view to show IMPDH's hydrophobicity. A as well as the can be shown as well.
Energy Transformation
As IMPDH has three nucleotide-binding sites, which aid in modulating and regulating catalytic activity, there is a large increase in affinity in this molecule. This more than likely comes from the simultaneous reduction of the entropic penalty of binding due to molecularity change.
</StructureSection>
References
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.
Hedstrom, Lizbeth. “IMP Dehydrogenase: Structure, Mechanism, and Inhibition.” Chemical Reviews, U.S. National Library of Medicine, July 2009, www.ncbi.nlm.nih.gov/pmc/articles/PMC2737513/.
