Universal capability of 3-ketosteroid Δ¹-dehydrogenases to catalyze Δ¹-dehydrogenation of C17-substituted steroids.

ABSTRACT:

Background

3-Ketosteroid Δ¹-dehydrogenases (KSTDs) are the enzymes involved in microbial cholesterol degradation and modification of steroids. They catalyze dehydrogenation between C1 and C2 atoms in ring A of the polycyclic structure of 3-ketosteroids. KSTDs substrate spectrum is broad, even though most of them prefer steroids with small substituents at the C17 atom. The investigation of the KSTD's substrate specificity is hindered by the poor solubility of the hydrophobic steroids in aqueous solutions. In this paper, we used 2-hydroxpropyl-β-cyclodextrin (HBC) as a solubilizing agent in a study of the KSTDs steady-state kinetics and demonstrated that substrate bioavailability has a pivotal impact on enzyme specificity.

Results

Molecular dynamics simulations on K

SUBMITTER: Wojcik P 

PROVIDER: S-EPMC8220720 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature