Mini-dialysis tubes as tools to prepare drug-protein adducts of P450-dependent reactive drug metabolites

Boerma, Jan Simon; Elias, Naura S.; Vermeulen, Nico; Commandeur, Jan N. M.

doi:10.1016/j.jpba.2014.10.025

Cited by 3 publications

(1 citation statement)

References 40 publications

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“…All positions of the P450 BM3 heme domain that have been mutated and show improvement toward drug/drug-like hydroxylation are shown (orange spheres). Mutated positions in the heme domain (residues 1–471) and in the reductase domain (472–1049) are listed, with refs: 8 (), 11 ( , ), 23 ( , ), 24 ( , ), 39 (), 47 ( , , , , , , , , − , , , , , , , , , − ), 49 ( , , , , , ), 51 ( , , , , , , − , , , , , ), 52 ( , , ), 58 ( , , , ), 64 ( , , , , , , , , , …”

Section: P450 Bm3 Variants Catalyzing Aromatic Hydroxylationmentioning

confidence: 99%

Choose Your Own Adventure: A Comprehensive Database of Reactions Catalyzed by Cytochrome P450 BM3 Variants

Fansher,

Besna,

Fendri

et al. 2024

ACS Catal.

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Cytochrome P450 BM3 monooxygenase is the topic of extensive research as many researchers have evolved this enzyme to generate a variety of products. However, the abundance of information on increasingly diversified variants of P450 BM3 that catalyze a broad array of chemistry is not in a format that enables easy extraction and interpretation. We present a database that categorizes variants by their catalyzed reactions and includes details about substrates to provide reaction context. This database of >1500 P450 BM3 variants is downloadable and machine-readable and includes instructions to maximize ease of gathering information. The database allows rapid identification of commonly reported substitutions, aiding researchers who are unfamiliar with the enzyme in identifying starting points for enzyme engineering. For those actively engaged in engineering P450 BM3, the database, along with this review, provides a powerful and user-friendly platform to understand, predict, and identify the attributes of P450 BM3 variants, encouraging the further engineering of this enzyme.

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