A sterol reductase responsible for the unusual 8(14)-unsaturation in bacterial sterol production and degradation
Alysha K. Lee, José-Luis Giner, Paula V. Welander · 2026
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Description
Alysha K Lee, José-Luis Giner, and Paula V Welander identify a bacterial enzyme behind an unusual sterol shape, in a 2026 study. Sterols such as cholesterol are vital lipids, and some bacteria make versions with a rare double-bond position. No protein was known to create that arrangement.
Working in a methane-eating bacterium, the team expressed candidate genes in a test system. One reductase enzyme reshaped the sterol core, reducing one bond and shifting another into the rare position. Changing single building blocks in the enzyme showed which parts grip and transform the sterol. The gene appears only in bacteria, mainly in a few families, and likely evolved alongside a partner enzyme.
Catalog record
| CREATOR | Alysha K. Lee, José-Luis Giner, Paula V. Welander |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 38 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |