Cytochromes P450 (CYPs) are enzymes that utilize heme as a cofactor to catalyze monooxygenase reactions. They belong to a superfamily of enzymes that have been identified in all kingdoms of life, including plants, animals, fungi, protists, bacteria, archaea, and even viruses. P450s are known for their remarkable ability to catalyze over 20 types of oxido-reduction reactions, making them "Nature's Most Versatile Biological Catalysts." However, despite the existence of more than 300,000 P450 genes in different databases, less than 0.2% of them have been functionally characterized.
    Building upon our previous work, we proudly present P450Rdb v2.0, a significantly expanded and deeply annotated resource of literature-supported P450 reactions. Compared to the first version (which contained 1,600 reactions, 600 P450s, and 200 species), the current 2.0 database catalogs 3,821 reactions involving 1,012 P450 enzymes across 374 species. Beyond merely expanding the dataset, v2.0 features a major leap in data depth: approximately 50% of the entries have been upgraded to include complete sets of substrates and products for the reactions, and around 30% are enriched with detailed experimental reaction conditions.
    Crucially, v2.0 introduces two major functional upgrades. The first is a Reaction Cascade module for visualizing multi-step metabolic networks. The second is an Enzyme-Substrate Prediction (ESP) model—a binary classifier specifically fine-tuned on our entire curated dataset to evaluate potential catalytic interactions. By empowering this comprehensive database with advanced AI tools, we aim to facilitate the discovery of new P450 functions, the design of novel drugs, and the development of cutting-edge biotechnologies.

Please cite us: P450Rdb: a manually curated database of reactions catalyzed by cytochrome P450 enzymes , Journal of Advanced Research, 2024, 63: 35-42, DOI: 10.1016/j.jare.2023.10.012