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Bacterial cytochrome P450-catalyzed regio- and stereoselective steroid hydroxylation enabled by directed evolution and rational design

Authors
  • Zhang, Xiaodong1
  • Peng, Yaqin1
  • Zhao, Jing1
  • Li, Qian1
  • Yu, Xiaojuan1
  • Acevedo-Rocha, Carlos G.2
  • Li, Aitao1
  • 1 Hubei University, Wuhan, 430062, People’s Republic of China , Wuhan (China)
  • 2 Biosyntia ApS, Copenhagen, 2100, Denmark , Copenhagen (Denmark)
Type
Published Article
Journal
Bioresources and Bioprocessing
Publisher
Springer Singapore
Publication Date
Jan 07, 2020
Volume
7
Issue
1
Identifiers
DOI: 10.1186/s40643-019-0290-4
Source
Springer Nature
Keywords
License
Green

Abstract

Steroids are the most widely marketed products by the pharmaceutical industry after antibiotics. Steroid hydroxylation is one of the most important functionalizations because their derivatives enable a higher biological activity compared to their less polar non-hydroxylated analogs. Bacterial cytochrome P450s constitute promising biocatalysts for steroid hydroxylation due to their high expression level in common workhorses like Escherichia coli. However, they often suffer from wrong or insufficient regio- and/or stereoselectivity, low activity, narrow substrate range as well as insufficient thermostability, which hampers their industrial application. Fortunately, these problems can be generally solved by protein engineering based on directed evolution and rational design. In this work, an overview of recent developments on the engineering of bacterial cytochrome P450s for steroid hydroxylation is presented.

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