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Induction of IMPDH-Based Cytoophidia by a Probable IMP-Dependent ARL13B-IMPDH Interaction.
Biochemistry (Mosc)
December 2024
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, 13145-1384, Iran.
Inosine Monophosphate Dehydrogenase (IMPDH) catalyzes rate-limiting step of the reaction converting inosine monophosphate (IMP) to guanine nucleotides. IMPDH is up-regulated in the healthy proliferating cells and also in tumor cells to meet their elevated demand for guanine nucleotides. An exclusive regulatory mechanism for this enzyme is filamentation, through which IMPDH can resist allosteric inhibition by the end product, GTP.
View Article and Find Full Text PDFDesuccinylation of inosine-5'-monophosphate dehydrogenase 1 by SIRT5 promotes tumor cell proliferation.
J Biol Chem
December 2024
Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, China. Electronic address:
Inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the rate limiting step of de novo purine synthesis. Currently, it remains still largely unknown how this metabolic event is regulated in tumor cells. Here, we report that a deacetylase sirtuin 5 (SIRT5) may possess a regulatory effect on GMP anabolism by desuccinylating IMPDH1.
View Article and Find Full Text PDFSynthesis, evaluation and mechanistic insights of novel IMPDH inhibitors targeting ESKAPEE bacteria.
Eur J Med Chem
December 2024
School of Chemistry, University College Cork, Cork, Ireland; School of Pharmacy, University College Cork, Cork, Ireland; Analytical and Biological Chemistry Research Facility, University College Cork, Cork, Ireland. Electronic address:
Antimicrobial resistance poses a significant threat to global health, necessitating the development of novel therapeutic agents with unique mechanisms of action. Inosine 5'-monophosphate dehydrogenase (IMPDH), an essential enzyme in guanine nucleotide biosynthesis, is a promising target for the discovery of new antimicrobial agents. High-throughput screening studies have previously identified several urea-based leads as potential inhibitors, although many of these are characterised by reduced chemical stability.
View Article and Find Full Text PDFDe novo GTP synthesis is a metabolic vulnerability for the interception of brain metastases.
Cell Rep Med
October 2024
Centre for Discovery in Cancer Research, McMaster University, Hamilton, ON, Canada; Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, ON, Canada; Department of Surgery, McMaster University, Hamilton, ON, Canada. Electronic address:
Patients with brain metastases (BM) face a 90% mortality rate within one year of diagnosis and the current standard of care is palliative. Targeting BM-initiating cells (BMICs) is a feasible strategy to treat BM, but druggable targets are limited. Here, we apply Connectivity Map analysis to lung-, breast-, and melanoma-pre-metastatic BMIC gene expression signatures and identify inosine monophosphate dehydrogenase (IMPDH), the rate-limiting enzyme in the de novo GTP synthesis pathway, as a target for BM.
View Article and Find Full Text PDFImpaired inosine monophosphate dehydrogenase leads to plant-specific ribosomal stress responses in Arabidopsis thaliana.
J Plant Res
November 2024
Department of Life Science, College of Science, Rikkyo University, Toshima, Tokyo, 171-8501, Japan.
Nucleotides are the building blocks of living organisms and their biosynthesis must be tightly regulated. Inosine monophosphate dehydrogenase (IMPDH) is a rate-limiting enzyme in GTP synthesis that is essential for biological activities, such as RNA synthesis. In animals, the suppression of IMPDH function causes ribosomal stress (also known as nucleolar stress), a disorder in ribosome biogenesis that results in cell proliferation defects and apoptosis.
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