ArticleScientific reports2017
Substrate recognition by two different P450s: Evidence for conserved roles in a common fold.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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.
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Who cites it
7 citing papers in PubMed.
- Tracking protein-protein interactions by NMR: conformational selection in human steroidogenic cytochrome P450 CYP17A1 induced by cytochromePhysical chemistry chemical physics : PCCP · 2024Article
- Conformational heterogeneity suggests multiple substrate binding modes in CYP106A2.Journal of inorganic biochemistry · 2023Article
- A dynamic understanding of cytochrome P450 structure and function through solution NMR.Current opinion in biotechnology · 2021Review
- Roles for Structural Biology in the Discovery of Drugs and Agrochemicals Targeting Sterol 14α-Demethylases.Journal of fungi (Basel, Switzerland) · 2021Review
- What Your Crystal Structure Will Not Tell You about Enzyme Function.Accounts of chemical research · 2019Article
- A new approach to understanding structure-function relationships in cytochromes P450 by targeting terpene metabolism in the wild.Journal of inorganic biochemistry · 2018Article
- Some Surprising Implications of NMR-directed Simulations of Substrate Recognition and Binding by Cytochrome P450Journal of molecular biology · 2018Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Cytochrome P450 monooxygenases CYP101A1 and MycG catalyze regio- and stereospecific oxidations of their respective substrates, d-camphor and mycinamicin IV. Despite the low sequence homology between the two enzymes (29% identity) and differences in size and hydrophobicity of their substrates, the conformational changes that occur upon substrate binding in both enzymes as determined by solution NMR methods show some striking similarities. Many of the same secondary structural features in both enzymes are perturbed, suggesting the existence of a common mechanism for substrate binding and recognition in the P450 superfamily.
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Registered trials
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