Literature DB >> 30991094

The role and mechanism of microbial 3-ketosteroid Δ1-dehydrogenases in steroid breakdown.

Ali Rohman1, Bauke W Dijkstra2.   

Abstract

3-Ketosteroid Δ1-dehydrogenases are FAD-dependent enzymes that catalyze the introduction of a double bond between the C1 and C2 atoms of the A-ring of 3-ketosteroid substrates. These enzymes are found in a large variety of microorganisms, especially in bacteria belonging to the phylum Actinobacteria. They play a critical role in the early steps of the degradation of the steroid core. 3-Ketosteroid Δ1-dehydrogenases are of particular interest for the etiology of some infectious diseases, for the production of starting materials for the pharmaceutical industry, and for environmental bioremediation applications. Here we summarize and discuss the biochemical and enzymological properties of these enzymes, their microbial sources, and their natural diversity. The three-dimensional structure of a 3-ketosteroid Δ1-dehydrogenase in connection with the enzyme mechanism is highlighted.
Copyright © 2019 The Authors. Published by Elsevier Ltd.. All rights reserved.

Entities:  

Keywords:  1(2)-dehydrogenation; Enzyme mechanism; Flavoenzyme; Steroid biotransformation; Sterol degradation

Mesh:

Substances:

Year:  2019        PMID: 30991094     DOI: 10.1016/j.jsbmb.2019.04.015

Source DB:  PubMed          Journal:  J Steroid Biochem Mol Biol        ISSN: 0960-0760            Impact factor:   4.292


  7 in total

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

Authors:  Patrycja Wójcik; Michał Glanowski; Agnieszka M Wojtkiewicz; Ali Rohman; Maciej Szaleniec
Journal:  Microb Cell Fact       Date:  2021-06-23       Impact factor: 5.328

7.  A New 3-Ketosteroid-Δ1-Dehydrogenase with High Activity and Broad Substrate Scope for Efficient Transformation of Hydrocortisone at High Substrate Concentration.

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  7 in total

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