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

0578950 - ÚOCHB 2024 RIV CZ eng A - Abstrakt
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]
Grant CEP: GA MŠMT(CZ) LX22NPO5103
Výzkumná infrastruktura: CIISB II - 90127
Institucionální podpora: RVO:61388963
Klíčová slova: inosine-5′-monophosphate dehydrogenase (IMPDH) * mycobacterial infection
Obor OECD: 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.
Trvalý link: https://hdl.handle.net/11104/0347853