2. Academic Validation
  3. The identification of new substrates of human DHRS7 by molecular modeling and in vitro testing

The identification of new substrates of human DHRS7 by molecular modeling and in vitro testing

  • Int J Biol Macromol. 2017 Dec;105(Pt 1):171-182. doi: 10.1016/j.ijbiomac.2017.07.012.
Lucie Zemanová 1,  Palani Kirubakaran 2,  Ignacio Hernando Pato 1,  Hana Štambergová 1,  Jiří Vondrášek 3
Affiliations

Affiliations

  • 1 Department of Biochemical Sciences, Faculty of Pharmacy in Hradec Králové, Charles University in Prague, Czech Republic.
  • 2 Institute of Organic Chemistry and Biochemistry AS CR, Flemingovo nám. 2, Prague, Czech Republic.
  • 3 Institute of Organic Chemistry and Biochemistry AS CR, Flemingovo nám. 2, Prague, Czech Republic. Electronic address: [email protected].
PMID: 28687384 DOI: 10.1016/j.ijbiomac.2017.07.012
Abstract

Human DHRS7 (SDR34C1) is one of insufficiently described enzymes of the short-chain dehydrogenase/reductase superfamily. The members of this superfamily often play an important pato/physiological role in the human body, participating in the metabolism of diverse substrates (e.g. retinoids, Steroids, xenobiotics). A systematic approach to the identification of novel, physiological substrates of DHRS7 based on a combination of homology modeling, structure-based virtual screening and experimental evaluation has been used. Three novel substrates of DHRS7 (dihydrotestosterone, benzil and 4,4'-dimetylbenzil) have been described.

Keywords

DHRS7; Homology modeling; Molecular modeling; SDR superfamily; SDR34C1.

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