期刊
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
卷 102, 期 19, 页码 8153-8171出版社
SPRINGER
DOI: 10.1007/s00253-018-9239-3
关键词
Steroid hydroxylation; Cytochrome P450; 3-ketosteroid 9 alpha-hydroxylase; Steroid C25 dehydrogenase
资金
- Polish National Center of Science [SONATA UMO-2012/05/D/ST4/00277]
- ICSC PAS
- Deutsche Bundesstiftung Umwelt
- Russian Science Foundation [18-14-00361]
The steroid superfamily includes a wide range of compounds that are essential for living organisms of the animal and plant kingdoms. Structural modifications of steroids highly affect their biological activity. In this review, we focus on hydroxylation of steroids by bacterial hydroxylases, which take part in steroid catabolic pathways and play an important role in steroid degradation. We compare three distinct classes of metalloenzymes responsible for aerobic or anaerobic hydroxylation of steroids, namely: cytochrome P450, Rieske-type monooxygenase 3-ketosteroid 9 alpha-hydroxylase, and molybdenum-containing steroid C25 dehydrogenases. We analyze the available literature data on reactivity, regioselectivity, and potential application of these enzymes in organic synthesis of hydroxysteroids. Moreover, we describe mechanistic hypotheses proposed for all three classes of enzymes along with experimental and theoretical evidences, which have provided grounds for their formulation. In case of the 3-ketosteroid 9 alpha-hydroxylase, such a mechanistic hypothesis is formulated for the first time in the literature based on studies conducted for other Rieske monooxygenases. Finally, we provide comparative analysis of similarities and differences in the reaction mechanisms utilized by bacterial steroid hydroxylases.
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