Premium
A Mechanism of Efficient G6PD Inhibition by a Molecular Clip
Author(s) -
Kirsch Michael,
Talbiersky Peter,
Polkowska Jolanta,
Bastkowski Frank,
Schaller Torsten,
de Groot Herbert,
Klärner FrankGerrit,
Schrader Thomas
Publication year - 2009
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200806175
Subject(s) - cofactor , nicotinamide adenine dinucleotide , dehydrogenase , chemistry , substrate (aquarium) , enzyme , nicotinamide adenine dinucleotide phosphate , biochemistry , nad+ kinase , mechanism (biology) , stereochemistry , biology , physics , quantum mechanics , ecology , oxidase test
Triple duty : A synthetic molecular clip traps nicotinamide adenine dinucleotide phosphate (NADP + ; see picture) as well as occupying both the cofactor‐ and the substrate‐binding site in glucose‐6‐phosphate (G6P) dehydrogenase. This combination of two inhibition mechanisms makes the clip highly effective and selective for this enzyme over other dehydrogenases.