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| | =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''== | | =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''== |
| | <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''> | | <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''> |
| - | This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
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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.
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| | == '''Function(s) and Biological Relevance''' == | | == '''Function(s) and Biological Relevance''' == |
Revision as of 01:33, 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 (IMPDH)
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Function(s) and Biological Relevance
Inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. [1]
Broader Implications
Structural highlights and structure-function relationships
Energy Transformation
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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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.
