Monooxygenase-mediated cascade oxidation of fatty acids for the production of biopolymer building blocks

Sudheer, Pammidimarri D. V. N.; Chauhan, S. M. S.; Jeon, Wooyoung; Ahn, Jungoh; Choi, Kwon‐Young

doi:10.1007/s13399-021-01991-z

Cited by 4 publications

(1 citation statement)

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“…Given the attractive features of P450 BM3, the enzyme has garnered significant attention and has been the subject of numerous reviews highlighting its exceptional properties and characteristics. Reviews have been conducted on various aspects of P450 BM3, including structural and mechanistic details, − hydroxylation, ,,− pharmaceutical compound hydroxylation, ,− epoxidation, ,,, and carbene/nitrene transfer. ,,,,,,− Additionally, studies have explored the use of decoy molecules to improve enzymatic activity, ,,,,,,− as well as P450 BM3-inorganic complexes. − Reviews of P450 BM3 frequently place it within a broader context of other P450 enzymes, resulting in a lack of focus. Though some reviews do describe reactions catalyzed by P450 BM3 variants, they are typically limited to discussion of the “best” variants for a given reaction and do not offer a comprehensive review of reported variants.…”

Section: P450 Bm3: Properties and Limitationsmentioning

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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