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In Silico Studies of Mammalian δ‐ALAD Interactions with Selenides and Selenoxides
Author(s) -
Andrei Nogara Pablo,
Batista Teixeira Rocha João
Publication year - 2018
Publication title -
molecular informatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.481
H-Index - 68
eISSN - 1868-1751
pISSN - 1868-1743
DOI - 10.1002/minf.201700091
Subject(s) - in silico , chemistry , dehydratase , active site , stereochemistry , electrophile , enzyme , combinatorial chemistry , biochemistry , catalysis , gene
Previous studies have shown that the mammalian δ‐aminolevulinic acid dehydratase (δ‐ALAD) is inhibited by selenides and selenoxides, which can involve thiol oxidation. However, the precise molecular interaction of selenides and selenoxides with the active center of the enzyme is unknown. Here, we try to explain the interaction of selenides and the respective selenoxides with human δ‐ALAD by in silico molecular docking. The in silico data indicated that Se atoms of selenoxides have higher electrophilic character than their respective selenides. Further, the presence of oxygen increased the interaction of selenoxides with the δ‐ALAD active site by O…Zn coordination. The interaction of S atom from Cys124 with the Se atom indicated the importance of the nucleophilic attack of the enzyme thiolate to the organoselenium molecules. These observations help us to understand the interaction of target proteins with organoselenium compounds.