Cytochrome P450 enzymes: understanding the biochemical hieroglyphs [v1; ref status: indexed, http://f1000r.es/583]

Cytochrome P450 (CYP) enzymes are the primary proteins of drug metabolism and steroid biosynthesis. These crucial proteins have long been known to harbor a cysteine thiolate bound to the heme iron. Recent advances in the field have illuminated the nature of reactive intermediates in the reaction cyc...

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Main Author: John T. Groves
Format: Article
Language:English
Published: F1000 Research Ltd 2015-07-01
Series:F1000Research
Subjects:
Online Access:http://f1000research.com/articles/4-178/v1
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author John T. Groves
author_facet John T. Groves
author_sort John T. Groves
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description Cytochrome P450 (CYP) enzymes are the primary proteins of drug metabolism and steroid biosynthesis. These crucial proteins have long been known to harbor a cysteine thiolate bound to the heme iron. Recent advances in the field have illuminated the nature of reactive intermediates in the reaction cycle. Similar intermediates have been observed and characterized in novel heme-thiolate proteins of fungal origin. Insights from these discoveries have begun to solve the riddle of how enzyme biocatalyst design can afford a protein that can transform substrates that are more difficult to oxidize than the surrounding protein architecture.
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spelling doaj.art-dfeb1f3d53e54769a9bc06997f9f224a2022-12-21T19:26:55ZengF1000 Research LtdF1000Research2046-14022015-07-01410.12688/f1000research.6314.16771Cytochrome P450 enzymes: understanding the biochemical hieroglyphs [v1; ref status: indexed, http://f1000r.es/583]John T. Groves0Department of Chemistry, Princeton University, Princeton, NJ, 08544, USACytochrome P450 (CYP) enzymes are the primary proteins of drug metabolism and steroid biosynthesis. These crucial proteins have long been known to harbor a cysteine thiolate bound to the heme iron. Recent advances in the field have illuminated the nature of reactive intermediates in the reaction cycle. Similar intermediates have been observed and characterized in novel heme-thiolate proteins of fungal origin. Insights from these discoveries have begun to solve the riddle of how enzyme biocatalyst design can afford a protein that can transform substrates that are more difficult to oxidize than the surrounding protein architecture.http://f1000research.com/articles/4-178/v1BiocatalysisBioinorganic ChemistryBiomacromolecule-Ligand InteractionsCancer TherapeuticsChemical Biology of the CellDrug Discovery & DesignExperimental Biophysical MethodsProtein Chemistry & Proteomics
spellingShingle John T. Groves
Cytochrome P450 enzymes: understanding the biochemical hieroglyphs [v1; ref status: indexed, http://f1000r.es/583]
F1000Research
Biocatalysis
Bioinorganic Chemistry
Biomacromolecule-Ligand Interactions
Cancer Therapeutics
Chemical Biology of the Cell
Drug Discovery & Design
Experimental Biophysical Methods
Protein Chemistry & Proteomics
title Cytochrome P450 enzymes: understanding the biochemical hieroglyphs [v1; ref status: indexed, http://f1000r.es/583]
title_full Cytochrome P450 enzymes: understanding the biochemical hieroglyphs [v1; ref status: indexed, http://f1000r.es/583]
title_fullStr Cytochrome P450 enzymes: understanding the biochemical hieroglyphs [v1; ref status: indexed, http://f1000r.es/583]
title_full_unstemmed Cytochrome P450 enzymes: understanding the biochemical hieroglyphs [v1; ref status: indexed, http://f1000r.es/583]
title_short Cytochrome P450 enzymes: understanding the biochemical hieroglyphs [v1; ref status: indexed, http://f1000r.es/583]
title_sort cytochrome p450 enzymes understanding the biochemical hieroglyphs v1 ref status indexed http f1000r es 583
topic Biocatalysis
Bioinorganic Chemistry
Biomacromolecule-Ligand Interactions
Cancer Therapeutics
Chemical Biology of the Cell
Drug Discovery & Design
Experimental Biophysical Methods
Protein Chemistry & Proteomics
url http://f1000research.com/articles/4-178/v1
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