PXD053345 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | Ring A cleaving beta-diketon hydrolase is a key enzyme of steroid degradation in anaerobic bacteria |
| Description | Bacterial degradation of the ubiquitous and persistent steroids is important for their removal from the environment, particularly for the endocrine disrupting steroid sex hormones. While aerobic bacteria use oxygenases to attack non-activated C-H/C-C bonds of the isoprenoid side chain or the steran skeleton of steroids, initial studies of steroid degradation in anaerobic bacteria suggested that water-dependent enzymes are involved in C-H hydroxylation and ring cleavage reactions. In anaerobic steroid catabolism, the hydrolytic enzymes involved in the cleavage of the steran ring system of the common intermediate androst-1,4-diene-3-one have remained unknown. Here, we have enriched a hydrolase from the cholesterol/nitrate grown Sterolibacterium denitrificans and from Escherichia coli after heterologous expression of its gene. It specifically cleaves the cyclic 1,3-diketone degradation intermediate of ring A, androsta-1,4,17-trione, to 1,17-dioxo-2,3-seco-androstan-3-oate (DSAO), a hallmark reaction of anaerobic steroid degradation. The highly conserved ring A hydrolase was identified in all known and many previously unknown steroid-degrading Proteobacteria. Using the enriched enzyme, we enzymatically produced the CoA ester of DSAO from the chemically synthesized androst-1-ene-3-one precursor, allowing the identification of subsequent metabolites involved in ring A degradation. The results obtained suggest the involvement of an additional hydrolase, an aldolase, and a -oxidation-like cascade for complete ring A degradation during which acetate and acetyl-CoA are released to form the three-ring 5,10-seco-1,2,3,4-tetranorandrosta-5,17-dione. The results identified a key enzyme of anaerobic steroid degradation that may serve as functional marker for monitoring steroid contaminant degradation at anoxic environmental sites. |
| HostingRepository | PRIDE |
| AnnounceDate | 2025-05-07 |
| AnnouncementXML | Submission_2025-05-06_20:02:06.448.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Lina Peller |
| SpeciesList | scientific name: Sterolibacterium denitrificans; NCBI TaxID: 157592; |
| ModificationList | No PTMs are included in the dataset |
| Instrument | Synapt MS |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
| 0 | 2024-06-24 01:58:48 | ID requested | |
| ⏵ 1 | 2025-05-06 20:02:07 | announced | |
Publication List
| Jacoby C, Peller L, Wenzler J, Luttermann M, Seiche W, Breit B, Boll M, Ring A Cleaving Beta-Diketone Hydrolase Is a Key Enzyme of Steroid Degradation in Anaerobic Bacteria. Environ Microbiol, 27(1):e70034(2025) [pubmed] |
| 10.1111/1462-2920.70034; |
Keyword List
| submitter keyword: Steroid degradation, LC-MS, Hydrolase,Sterolibacterium denitrificans |
Contact List
| Matthias Boll |
| contact affiliation | Faculty of Biology - Microbiology, University of Freiburg,79104 Freiburg, Germany |
| contact email | matthias.boll@biologie.uni-freiburg.de |
| lab head | |
| Lina Peller |
| contact affiliation | University of Freiburg |
| contact email | lina.peller@biologie.uni-freiburg.de |
| dataset submitter | |
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/05/PXD053345 |
| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD053345
- Label: PRIDE project
- Name: Ring A cleaving beta-diketon hydrolase is a key enzyme of steroid degradation in anaerobic bacteria