ArticleBiochemistry2012
Bacillus anthracis inosine 5'-monophosphate dehydrogenase in action: the first bacterial series of structures of phosphate ion-, substrate-, and product-bound complexes.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Deciphering the allosteric regulation of mycobacterial inosine-5'-monophosphate dehydrogenase.Nature communications · 2024Article
- A journey into the regulatory secrets of theFrontiers in pharmacology · 2024Review
- Combining multi-omics analysis to identify host-targeted targets for the control of Brucella infection.Microbial biotechnology · 2023Article
- The gateway to guanine nucleotides: Allosteric regulation of IMP dehydrogenases.Protein science : a publication of the Protein Society · 2022Review
- Diadenosine tetraphosphate regulates biosynthesis of GTP in Bacillus subtilis.Nature microbiology · 2022Article
- The Enzymatic Activity of Inosine 5'-Monophosphate Dehydrogenase May Not Be a Vulnerable Target forACS infectious diseases · 2021Article
- Evaluation of Bronopol and Disulfiram as PotentialMolecules (Basel, Switzerland) · 2020Article
- In cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of genuine co-factors.Nature communications · 2020Article
- Inhibitors of inosine 5'-monophosphate dehydrogenase as emerging new generation antimicrobial agents.MedChemComm · 2019Review
- Oxanosine Monophosphate Is a Covalent Inhibitor of Inosine 5'-Monophosphate Dehydrogenase.Chemical research in toxicology · 2019Article
- Redox regulation by reversible protein S-thiolation in Gram-positive bacteria.Redox biology · 2019Review
- Precision therapeutic targeting of human cancer cell motility.Nature communications · 2018Article
- Expanding Benzoxazole-Based Inosine 5'-Monophosphate Dehydrogenase (IMPDH) Inhibitor Structure-Activity As Potential Antituberculosis Agents.Journal of medicinal chemistry · 2018Article
- Structure of the Bacillus anthracis dTDP-l-rhamnose biosynthetic pathway enzyme: dTDP-α-d-glucose 4,6-dehydratase, RfbB.Journal of structural biology · 2018Article
- Fragment-Based Approach to Targeting Inosine-5'-monophosphate Dehydrogenase (IMPDH) from Mycobacterium tuberculosis.Journal of medicinal chemistry · 2018Article
- A nucleotide-controlled conformational switch modulates the activity of eukaryotic IMP dehydrogenases.Scientific reports · 2017Article
- Inhibition of Inosine-5'-monophosphate Dehydrogenase from Bacillus anthracis: Mechanism Revealed by Pre-Steady-State Kinetics.Biochemistry · 2016Article
- Guanine nucleotide binding to the Bateman domain mediates the allosteric inhibition of eukaryotic IMP dehydrogenases.Nature communications · 2015Article
- Structural Genomics Support for Infectious Disease Drug Design.ACS infectious diseases · 2015Article
- A novel cofactor-binding mode in bacterial IMP dehydrogenases explains inhibitor selectivity.The Journal of biological chemistry · 2015Article
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17 authors.
Funding
Abstract
Inosine 5'-monophosphate dehydrogenase (IMPDH) catalyzes the first unique step of the GMP branch of the purine nucleotide biosynthetic pathway. This enzyme is found in organisms of all three kingdoms. IMPDH inhibitors have broad clinical applications in cancer treatment, as antiviral drugs and as immunosuppressants, and have also displayed antibiotic activity. We have determined three crystal structures of Bacillus anthracis IMPDH, in a phosphate ion-bound (termed "apo") form and in complex with its substrate, inosine 5'-monophosphate (IMP), and product, xanthosine 5'-monophosphate (XMP). This is the first example of a bacterial IMPDH in more than one state from the same organism. Furthermore, for the first time for a prokaryotic enzyme, the entire active site flap, containing the conserved Arg-Tyr dyad, is clearly visible in the structure of the apoenzyme. Kinetic parameters for the enzymatic reaction were also determined, and the inhibitory effect of XMP and mycophenolic acid (MPA) has been studied. In addition, the inhibitory potential of two known Cryptosporidium parvum IMPDH inhibitors was examined for the B. anthracis enzyme and compared with those of three bacterial IMPDHs from Campylobacter jejuni, Clostridium perfringens, and Vibrio cholerae. The structures contribute to the characterization of the active site and design of inhibitors that specifically target B. anthracis and other microbial IMPDH enzymes.
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