Deciphering the allosteric regulation of mycobacterial inosine-5′-monophosphate dehydrogenase
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F23%3A00578950" target="_blank" >RIV/61388963:_____/23:00578950 - isvavai.cz</a>
Result on the web
<a href="http://www.ccsss.cz/index.php/ccsss/issue/view/41/75" target="_blank" >http://www.ccsss.cz/index.php/ccsss/issue/view/41/75</a>
DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Deciphering the allosteric regulation of mycobacterial inosine-5′-monophosphate dehydrogenase
Original language description
Inosine-5′-monophosphate dehydrogenase (IMPDH) is acrucial purine metabolism enzyme that is considered a promising drug target against mycobacterial infections. IMPDH catalyzes the NAD-dependent oxidation of inosine-5′-monophosphate (IMP) to xanthosine 5′-monophosphate (XMP) a first committed step in the biosynthesis of guanine nucleotides. Regulation of IMPDH enzymatic activity is therefore crucial for cell survival. Despite recent advances in understanding the regulation in other bacteria, little is known about the allosteric regulation of mycobacterial IMPDH.
Czech name
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Czech description
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Classification
Type
O - Miscellaneous
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/LX22NPO5103" target="_blank" >LX22NPO5103: National Institute of Virology and Bacteriology</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2023
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů