ReviewChemical Society reviews2021
Racemases and epimerases operating through a 1,1-proton transfer mechanism: reactivity, mechanism and inhibition.
Review in Chemical Society reviews, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 26 citations in OpenAlex.
- Recent progress in microbial production of D-aspartate.World journal of microbiology & biotechnology · 2026Review
- Ornithine racemase uses a catalytic cysteine.Biochimica et biophysica acta. Proteins and proteomics · 2026Article
- Mechanistic Elucidation and Stereochemical Consequences of Alternative Binding of Alkenyl Substrates by Engineered Arylmalonate Decarboxylase.Journal of the American Chemical Society · 2025Article
- Structure and inhibition of diaminopimelic acid epimerase by slow-binding α-methyl amino acids.Protein science : a publication of the Protein Society · 2025Article
- Structural and Functional Basis of GenB2 Isomerase Activity from Gentamicin Biosynthesis.ACS chemical biology · 2024Article
- Synthetic techniques for thermodynamically disfavoured substituted six-membered rings.Nature reviews. Chemistry · 2024Review
- α-Methylacyl-CoA Racemase fromBiomolecules · 2024Article
- A stereochemical journey around spirocyclic glutamic acid analogs.Organic & biomolecular chemistry · 2022Article
- The Unexplored Importance of Fleeting Chiral Intermediates in Enzyme-Catalyzed Reactions.Journal of the American Chemical Society · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Racemases and epimerases catalyse changes in the stereochemical configurations of chiral centres and are of interest as model enzymes and as biotechnological tools. They also occupy pivotal positions within metabolic pathways and, hence, many of them are important drug targets. This review summarises the catalytic mechanisms of PLP-dependent, enolase family and cofactor-independent racemases and epimerases operating by a deprotonation/reprotonation (1,1-proton transfer) mechanism and methods for measuring their catalytic activity. Strategies for inhibiting these enzymes are reviewed, as are specific examples of inhibitors. Rational design of inhibitors based on substrates has been extensively explored but there is considerable scope for development of transition-state mimics and covalent inhibitors and for the identification of inhibitors by high-throughput, fragment and virtual screening approaches. The increasing availability of enzyme structures obtained using X-ray crystallography will facilitate development of inhibitors by rational design and fragment screening, whilst protein models will facilitate development of transition-state mimics.
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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.