ArticleJournal of the American Chemical Society2012
Insights into the mechanistic dichotomy of the protein farnesyltransferase peptide substrates CVIM and CVLS.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Protein farnesylation: from molecular mechanisms to therapeutic targeting in cancer, aging, and beyond.Frontiers in pharmacology · 2026Review
- Role of substrate dynamics in protein prenylation reactions.Accounts of chemical research · 2015Review
- Protein prenylation: enzymes, therapeutics, and biotechnology applications.ACS chemical biology · 2015Review
- Origin of product selectivity in a prenyl transfer reaction from the same intermediate: exploration of multiple FtmPT1-catalyzed prenyl transfer pathways.Biochemistry · 2014Article
- Understanding a substrate's product regioselectivity in a family of enzymes: a case study of acetaminophen binding in cytochrome P450s.PloS one · 2014Article
- Solution NMR refinement of a metal ion bound protein using metal ion inclusive restrained molecular dynamics methods.Journal of biomolecular NMR · 2013Article
- Prenyltransferase Inhibitors: Treating Human Ailments from Cancer to Parasitic Infections.MedChemComm · 2013Article
- Recent advances in protein prenyltransferases: substrate identification, regulation, and disease interventions.Current opinion in chemical biology · 2012Review
- Farnesyl diphosphate analogues with aryl moieties are efficient alternate substrates for protein farnesyltransferase.Biochemistry · 2012Article
- Catalytic mechanism of aromatic prenylation by NphB.Biochemistry · 2012Article
- Solution structure of Mycobacterium tuberculosis NmtR in the apo state: insights into Ni(II)-mediated allostery.Biochemistry · 2012Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Protein farnesyltransferase (FTase) catalyzes farnesylation of a variety of peptide substrates. (3)H α-secondary kinetic isotope effect (α-SKIE) measurements of two peptide substrates, CVIM and CVLS, are significantly different and have been proposed to reflect a rate-limiting S(N)2-like transition state with dissociative characteristics for CVIM, while, due to the absence of an isotope effect, CVLS was proposed to have a rate-limiting peptide conformational change. Potential of mean force quantum mechanical/molecular mechanical studies coupled with umbrella sampling techniques were performed to further probe this mechanistic dichotomy. We observe the experimentally proposed transition state (TS) for CVIM but find that CVLS has a symmetric S(N)2 TS, which is also consistent with the absence of a (3)H α-SKIE. These calculations demonstrate facile substrate-dependent alterations in the transition state structure catalyzed by FTase.
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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.