ArticleScientific reports2021
Surface hydrophobics mediate functional dimerization of CYP121A1 of Mycobacterium tuberculosis.
Article in Scientific reports, 2021. 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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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Characterization of a CYP107 family vitamin DArchives of biochemistry and biophysics · 2026Article
- 3-(Pyridine-3-ylmethylene)chroman-4-one and tetralone derivatives: synthesis,RSC medicinal chemistry · 2026Article
- Recent Characterization of Key Proteins to Combat Tuberculosis.Advances in experimental medicine and biology · 2026Review
- Active Site Residues Contribute to the Multistep Dynamics of Dicyclotyrosine Bound to CYP121A1 ofBiochemistry · 2025Article
- In Situ Structural Observation of a Substrate- and Peroxide-Bound High-Spin Ferric-Hydroperoxo Intermediate in the P450 Enzyme CYP121.Journal of the American Chemical Society · 2023Article
- Synthesis, biological evaluation and computational studies of pyrazole derivatives asRSC medicinal chemistry · 2022Article
- Structural, energetic and lipophilic analysis of SARS-CoV-2 non-structural protein 9 (NSP9).Scientific reports · 2021Article
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
Tuberculosis is caused by the pathogenic bacterium Mycobacterium tuberculosis (Mtb) and remains the leading cause of death by infection world-wide. The Mtb genome encodes a disproportionate number of twenty cytochrome P450 enzymes, of which the essential enzyme cytochrome P450 121A1 (CYP121A1) remains a target of drug design efforts. CYP121A1 mediates a phenol coupling reaction of the tyrosine dipeptide cyclo-L-Tyr-L-Tyr (cYY). In this work, a structure and function investigation of dimerization was performed as an overlooked feature of CYP121A1 function. This investigation showed that CYP121A1 dimers form via intermolecular contacts on the distal surface and are mediated by a network of solvent-exposed hydrophobic residues. Disruption of CYP121A1 dimers by site-directed mutagenesis leads to a partial loss of specificity for cYY, resulting in an approximate 75% decrease in catalysis.
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Registered trials
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