ArticleThe journal of physical chemistry. B2015
Enzyme homologues have distinct reaction paths through their transition states.
Article in The journal of physical chemistry. B, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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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
10 citing papers in PubMed.
- Atomistic description of the relationship between protein dynamics and catalysis with transition path sampling.Methods in enzymology · 2023Review
- Perspective: Path Sampling Methods Applied to Enzymatic Catalysis.Journal of chemical theory and computation · 2022Review
- Multiple Reaction Pathways in the Morphinone Reductase-Catalyzed Hydride Transfer Reaction.ACS omega · 2020Article
- Examining the Origin of Catalytic Power of Catechol O-Methyltransferase.ACS catalysis · 2019Article
- Optimization of the Turnover in Artificial Enzymes via Directed Evolution Results in the Coupling of Protein Dynamics to Chemistry.Journal of the American Chemical Society · 2019Article
- Incorporating Fast Protein Dynamics into Enzyme Design: A Proposed Mutant Aromatic Amine Dehydrogenase.The journal of physical chemistry. B · 2017Article
- Resolution of Submillisecond Kinetics of Multiple Reaction Pathways for Lactate Dehydrogenase.Biophysical journal · 2017Article
- Neutron structures of the Helicobacter pylori 5'-methylthioadenosine nucleosidase highlight proton sharing and protonation states.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- What Mutagenesis Can and Cannot Reveal About Allostery.Biophysical journal · 2016Review
- Modulating Enzyme Catalysis through Mutations Designed to Alter Rapid Protein Dynamics.Journal of the American Chemical Society · 2016Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Recent studies of the bacterial enzymes EcMTAN and VcMTAN showed that they have different binding affinities for the same transition state analogue. This was surprising given the similarity of their active sites. We performed transition path sampling simulations of both enzymes to reveal the atomic details of the catalytic chemical step, which may be the key for explaining the inhibitor affinity differences. Even though all experimental data would suggest the two enzymes are almost identical, subtle dynamic differences manifest in differences of reaction coordinate, transition state structure, and eventually significant differences in inhibitor binding. Unlike EcMTAN, VcMTAN has multiple distinct transition states, which is an indication that multiple sets of coordinated protein motions can reach a transition state. Reaction coordinate information is only accessible from transition path sampling approaches, since all experimental approaches report averages. Detailed knowledge could have a significant impact on pharmaceutical design.
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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.