ArticleNature chemical biology2011
Cofactor mobility determines reaction outcome in the IMPDH and GMPR (β-α)8 barrel enzymes.
Article in Nature chemical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 36 citations in OpenAlex.
- Characterization of Recombinant GMPR fromBiology · 2026Article
- Structural basis for allosteric regulation of mycobacterial guanosine 5´-monophosphate reductase by ATP and GTP.Nature communications · 2026Article
- Effect on cell survival and cytoophidium assembly of the adRP-10-related IMPDH1 missense mutation Asp226Asn.Frontiers in cell and developmental biology · 2023Article
- The mycobacterial guaB1 gene encodes a guanosine 5'-monophosphate reductase with a cystathionine-β-synthase domain.The FEBS journal · 2022Article
- Phosphorylation of guanosine monophosphate reductase triggers a GTP-dependent switch from pro- to anti-oncogenic function of EPHA4.Cell chemical biology · 2022Article
- High ResolutionFrontiers in molecular biosciences · 2022Review
- Hydride Abstraction as the Rate-Limiting Step of the Irreversible Inhibition of Monoamine Oxidase B by Rasagiline and Selegiline: A Computational Empirical Valence Bond Study.International journal of molecular sciences · 2020Article
- Enzyme-Substrate-Cofactor Dynamical Networks Revealed by High-Resolution Field Cycling Relaxometry.Biochemistry · 2020Article
- Repurposing existing drugs: identification of irreversible IMPDH inhibitors by high-throughput screening.Journal of enzyme inhibition and medicinal chemistry · 2019Article
- Dynamic Characteristics of Guanosine-5'-monophosphate Reductase Complexes Revealed by High-ResolutionBiochemistry · 2018Article
- IMP/GTP balance modulates cytoophidium assembly and IMPDH activity.Cell division · 2018Article
- Substrate and Cofactor Dynamics on Guanosine Monophosphate Reductase Probed by High Resolution Field Cycling 31P NMR Relaxometry.The Journal of biological chemistry · 2016Article
- Molecular Basis of C-N Bond Cleavage by the Glycyl Radical Enzyme Choline Trimethylamine-Lyase.Cell chemical biology · 2016Article
- The cystathionine-β-synthase domains on the guanosine 5''-monophosphate reductase and inosine 5'-monophosphate dehydrogenase enzymes from Leishmania regulate enzymatic activity in response to guanylate and adenylate nucleotide levels.Molecular microbiology · 2016Article
- Novel Characteristics of Trypanosoma brucei Guanosine 5'-monophosphate Reductase Distinct from Host Animals.PLoS neglected tropical diseases · 2016Article
- A novel cofactor-binding mode in bacterial IMP dehydrogenases explains inhibitor selectivity.The Journal of biological chemistry · 2015Article
- A facile and sensitive method for quantification of cyclic nucleotide monophosphates in mammalian organs: basal levels of eight cNMPs and identification of 2',3'-cIMP.Biomolecules · 2014Article
- Quantum-chemical approach to determining the high potency of clorgyline as an irreversible acetylenic monoamine oxidase inhibitor.Journal of neural transmission (Vienna, Austria : 1996) · 2013Article
- Helicobacter pylori relies primarily on the purine salvage pathway for purine nucleotide biosynthesis.Journal of bacteriology · 2012Article
- The dynamic determinants of reaction specificity in the IMPDH/GMPR family of (β/α)(8) barrel enzymes.Critical reviews in biochemistry and molecular biologyReview
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Authors and funding
12 authors at 5 institutions in 4 countries.
Funding
Abstract
Inosine monophosphate dehydrogenase (IMPDH) and guanosine monophosphate reductase (GMPR) belong to the same structural family, share a common set of catalytic residues and bind the same ligands. The structural and mechanistic features that determine reaction outcome in the IMPDH and GMPR family have not been identified. Here we show that the GMPR reaction uses the same intermediate E-XMP* as IMPDH, but in this reaction the intermediate reacts with ammonia instead of water. A single crystal structure of human GMPR type 2 with IMP and NADPH fortuitously captures three different states, each of which mimics a distinct step in the catalytic cycle of GMPR. The cofactor is found in two conformations: an 'in' conformation poised for hydride transfer and an 'out' conformation in which the cofactor is 6 Å from IMP. Mutagenesis along with substrate and cofactor analog experiments demonstrate that the out conformation is required for the deamination of GMP. Remarkably, the cofactor is part of the catalytic machinery that activates ammonia.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.