ArticleThe Journal of biological chemistry2026
Supporting activities of cognate redox partners for sterol-metabolizing P450 enzymes in Mycobacterium neoaurum.
Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Steroids with anti-inflammatory, anti-allergic, endocrine-regulating, and other pharmaceutical activities represent the second most widely used class of drugs worldwide, following antibiotics. Their industrial production primarily relies on Mycobacteria-mediated biotransformation of sterols into key intermediates, followed by chemical or enzymatic modifications. While the sterol metabolic pathways in Mycobacteria have been intensively studied, the identification and functional characterization of key enzymes, particularly cytochrome P450 enzymes (CYPs or P450s) and their cognate redox partners, remain incomplete. Here, we heterologously expressed 24 P450s, 10 ferredoxin reductases (FdRs), and 12 ferredoxins (Fdxs) from Mycobacterium neoaurum ZC-1 in Escherichia coli. In vitro biochemical experiments identified five P450 enzymes (CYP125A76, CYP125A77, CYP125A78, CYP142A12, and CYP124A1) capable of catalyzing sterol side-chain terminal oxidation. Screening 120 redox partner combinations revealed FdR4662/Fdx4443 as the optimal cognate redox partners for all five P450 enzymes. With this redox partner pair, CYP142A12 achieved a conversion ratio of 89% for 4-cholesten-3-one with NADH as the preferred cofactor. Structural analyses indicate that the electron-transfer efficiency is primarily governed by electrostatic complementarity around the Fe-S cluster, the redox-center distance between the Fe-S cluster and heme-iron, and the FAD-to-cluster distance within the FdR-Fdx complex. These findings highlight the critical role of redox partner selection in enhancing P450 catalytic efficiency and provide a solid foundation for engineering high-efficiency industrial strains to improve steroid biomanufacturing and reduce production costs.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.