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

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,...

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Published inInternational journal of biological macromolecules Vol. 105; no. Pt 1; pp. 171 - 182
Main Authors Zemanová, Lucie, Kirubakaran, Palani, Pato, Ignacio Hernando, Štambergová, Hana, Vondrášek, Jiří
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.12.2017
Subjects
DHRS7
Dihydrotestosterone - metabolism
Homology modeling
Humans
Molecular Docking Simulation
Molecular modeling
Oxidoreductases - chemistry
Oxidoreductases - metabolism
Phenylglyoxal - analogs & derivatives
Phenylglyoxal - metabolism
Protein Binding
Protein Conformation
SDR superfamily
SDR34C1
DHRS7
SDR34C1
SDR superfamily
Molecular modeling
Homology modeling
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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2017.07.012