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Studies of Inhibitor Binding to the [4Fe‐4S] Cluster of Quinolinate Synthase
Author(s) -
Chan Alice,
Clémancey Martin,
Mouesca JeanMarie,
Amara Patricia,
Hamelin Olivier,
Latour JeanMarc,
Ollagnier de Choudens Sandrine
Publication year - 2012
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.201202261
Subject(s) - quinolinate , nad+ kinase , biosynthesis , nicotinamide adenine dinucleotide , biochemistry , quinolinic acid , enzyme , chemistry , atp synthase , stereochemistry , nicotinamide , tryptophan , amino acid
Stop for NadA! A [4Fe‐4S] enzyme, NadA, catalyzes the formation of quinolinic acid in de novo nicotinamide adenine dinucleotide (NAD) biosynthesis. A structural analogue of an intermediate, 4,5‐dithiohydroxyphthalic acid (DTHPA), has an in vivo NAD biosynthesis inhibiting activity in E. coli. The inhibitory effect can be explained by the coordination of DTHPA thiolate groups to a unique Fe site of the NadA [4Fe‐4S] cluster.