Dataset Information

Wild type enrichment of a 25-phospho-steroid kinase involved in anaerobic steroid degradation

ABSTRACT: The anaerobic degradation of cholesterol fundamentally differs from the cytochrome P450 monooxygenase dependent activation of the isoprenoid side chain at C26 in aerobes. In the denitrifying β-proteobacterium Sterolibacterium denitrificans, activation of primary C26 proceeds via a three-step cascade involving (i) a water-dependent hydroxylation at tertiary C25, (ii) an ATP-dependent dehydration to an alkene, and (iii) a water-dependent hydroxylation at primary C26 to an allylic alcohol. Here, we enriched a 25-hydroxy-steroid kinase (25-HSK) from Sterolibacterium denitrificans that catalyses the ATP-dependent transformation of 25-OH-cholest-1,4-diene-3-one (25-OH-CDO) to 25-phospho-CDO.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Sterolibacterium Denitrificans

SUBMITTER: Christian Jacoby

LAB HEAD: Matthias Boll

PROVIDER: PXD027031 | Pride | 2022-02-17

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	20210624_RGCJ_1.mgf	Mgf
	20210624_RGCJ_1.raw.zip	Raw
	20210624_RGCJ_1_Sterolibacterium_Workflow_2.mzid.gz	Mzid
	20210624_RGCJ_2.mgf	Mgf
	20210624_RGCJ_2.raw.zip	Raw

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Publications

A fully reversible 25-hydroxy steroid kinase involved in oxygen-independent cholesterol side-chain oxidation.

Jacoby Christian C Goerke Malina M Bezold Dominik D Jessen Henning H Boll Matthias M

The Journal of biological chemistry 20210821 4

The degradation of cholesterol and related steroids by microbes follows fundamentally different strategies in aerobic and anaerobic environments. In anaerobic bacteria, the primary C26 of the isoprenoid side chain is hydroxylated without oxygen via a three-step cascade: (i) water-dependent hydroxylation at the tertiary C25, (ii) ATP-dependent dehydration to form a subterminal alkene, and (iii) water-dependent hydroxylation at the primary C26 to form an allylic alcohol. However, the enzymes invol ...[more]

PMID: 34425106

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