Aerobic catabolism of sterols by microorganisms: key enzymes that open the 3-ketosteroid nucleus.
3-keto-4-en-steroid 5α-reductase
3-ketosteroid 9α-hydroxylase
3-ketosteroid C4-(5α)-dehydrogenase
3-ketosteroid Δ1-dehydrogenase
microorganisms
Journal
FEMS microbiology letters
ISSN: 1574-6968
Titre abrégé: FEMS Microbiol Lett
Pays: England
ID NLM: 7705721
Informations de publication
Date de publication:
01 07 2019
01 07 2019
Historique:
received:
30
04
2019
accepted:
06
08
2019
pubmed:
8
8
2019
medline:
17
6
2020
entrez:
8
8
2019
Statut:
ppublish
Résumé
Aerobic degradation of the sterol tetracyclic nucleus by microorganisms comprises the catabolism of A/B-rings, followed by that of C/D-rings. B-ring rupture at the C9,10-position is a key step involving 3-ketosteroid Δ1-dehydrogenase (KstD) and 3-ketosteroid 9α-hydroxylase (KstH). Their activities lead to the aromatization of C4,5-en-containing A-ring causing the rupture of B-ring. C4,5α-hydrogenated 3-ketosteroid could be produced by the growing microorganism containing a 5α-reductase. In this case, the microorganism synthesizes, in addition to KstD and KstH, a 3-ketosteroid Δ4-(5α)-dehydrogenase (Kst4D) in order to produce the A-ring aromatization, and consequently B-ring rupture. KstD and Kst4D are FAD-dependent oxidoreductases. KstH is composed of a reductase and a monooxygenase. This last component is the catalytic unit; it contains a Rieske-[2Fe-2S] center with a non-haem mononuclear iron in the active site. Published data regarding these enzymes are reviewed.
Identifiants
pubmed: 31390014
pii: 5544764
doi: 10.1093/femsle/fnz173
pii:
doi:
Substances chimiques
Ketosteroids
0
Sterols
0
Oxidoreductases
EC 1.-
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© FEMS 2019.