ArticleEnvironmental microbiology2013
A highly conserved mycobacterial cholesterol catabolic pathway.
Article in Environmental microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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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.
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Who cites it
24 citing papers in PubMed, 63 citations in OpenAlex.
- A sterol reductase responsible for the unusual 8(14)-unsaturation in bacterial sterol production and degradation.Journal of bacteriology · 2026Article
- A sterol reductase responsible for the unusual 8(14)-unsaturation in bacterial sterol production and degradation.bioRxiv : the preprint server for biology · 2026Article
- Structure-Function Analysis ofInternational journal of molecular sciences · 2025Article
- Unravelling and engineering an operon involved in the side-chain degradation of sterols in Mycolicibacterium neoaurum for the production of steroid synthons.Biotechnology for biofuels and bioproducts · 2023Article
- Structure Based Discovery of Inhibitors of CYP125 and CYP142 from Mycobacterium tuberculosis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Roles of cysteine in the structure and metabolic function ofRSC advances · 2022Article
- Genome-wide association studies of global Mycobacterium tuberculosis resistance to 13 antimicrobials in 10,228 genomes identify new resistance mechanisms.PLoS biology · 2022Article
- Microbial Steroid Production Technologies: Current Trends and Prospects.Microorganisms · 2021Article
- Whole-genome and enzymatic analyses of an androstenedione-producing Mycobacterium strain with residual phytosterol-degrading pathways.Microbial cell factories · 2020Article
- Unraveling the 17β-Estradiol Degradation Pathway inFrontiers in microbiology · 2020Article
- Comprehensive analysis of protein acetyltransferases of human pathogen Mycobacterium tuberculosis.Bioscience reports · 2019Article
- Distinct Physiological Roles of the Three Ferredoxins Encoded in the Hyperthermophilic ArchaeonmBio · 2019Article
- Comprehensive Comparative Analysis of Cholesterol Catabolic Genes/Proteins in Mycobacterial Species.International journal of molecular sciences · 2019Article
- Microenvironment ofBioMed research international · 2019Article
- Bacterial steroid hydroxylases: enzyme classes, their functions and comparison of their catalytic mechanisms.Applied microbiology and biotechnology · 2018Review
- System-wide coordinates of higher order functions in host-pathogen environment upon Mycobacterium tuberculosis infection.Scientific reports · 2018Article
- Potential drug targets in the Mycobacterium tuberculosis cytochrome P450 system.Journal of inorganic biochemistry · 2018Review
- Structural characterization of CYP144A1 - a cytochrome P450 enzyme expressed from alternative transcripts in Mycobacterium tuberculosis.Scientific reports · 2016Article
- Article
- Cytochrome P450 125A4, the Third Cholesterol C-26 Hydroxylase from Mycobacterium smegmatis.Biochemistry · 2015Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Degradation of the cholesterol side-chain in Mycobacterium tuberculosis is initiated by two cytochromes P450, CYP125A1 and CYP142A1, that sequentially oxidize C26 to the alcohol, aldehyde and acid metabolites. Here we report characterization of the homologous enzymes CYP125A3 and CYP142A2 from Mycobacterium smegmatis mc(2) 155. Heterologously expressed, purified CYP125A3 and CYP142A2 bound cholesterol, 4-cholesten-3-one, and antifungal azole drugs. CYP125A3 or CYP142A2 reconstituted with spinach ferredoxin and ferredoxin reductase efficiently hydroxylated 4-cholesten-3-one to the C-26 alcohol and subsequently to the acid. The X-ray structures of both substrate-free CYP125A3 and CYP142A2 and of cholest-4-en-3-one-bound CYP142A2 reveal significant differences in the substrate binding sites compared with the homologous M. tuberculosis proteins. Deletion only of cyp125A3 causes a reduction of both the alcohol and acid metabolites and a strong induction of cyp142 at the mRNA and protein levels, indicating that CYP142A2 serves as a functionally redundant back up enzyme for CYP125A3. In contrast to M. tuberculosis, the M. smegmatis Δcyp125Δcyp142 double mutant retains its ability to grow on cholesterol albeit with a diminished capacity, indicating an additional level of redundancy within its genome.
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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.