Deciphering the allosteric regulation of mycobacterial inosine-5′-monophosphate dehydrogenase

0578950 - ÚOCHB 2024 RIV CZ eng A - Abstract
Bulvas, Ondřej - Knejzlík, Zdeněk - Kouba, Tomáš - Pichová, Iva
Deciphering the allosteric regulation of mycobacterial inosine-5′-monophosphate dehydrogenase.
Czech Chemical Society Symposium Series. Roč. 21, č. 5 (2023), s. 180. ISSN 2336-7202.
[Annual meeting of the National Institute of Virology and Bacteriology (NIVB) /2./. 02.10.2023-05.10.2023, Kutná Hora]
R&D Projects: GA MŠMT(CZ) LX22NPO5103
Research Infrastructure: CIISB II - 90127
Institutional support: RVO:61388963
Keywords : inosine-5′-monophosphate dehydrogenase (IMPDH) * mycobacterial infection
OECD category: Biochemistry and molecular biology
http://www.ccsss.cz/index.php/ccsss/issue/view/41/75

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.
Permanent Link: https://hdl.handle.net/11104/0347853