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Studies of inhibitor binding to the [4Fe-4S] cluster of quinolinate synthase.
- Source :
-
Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 2012 Jul 27; Vol. 51 (31), pp. 7711-4. Date of Electronic Publication: 2012 Jun 19. - Publication Year :
- 2012
-
Abstract
- 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.<br /> (Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)
- Subjects :
- Alkyl and Aryl Transferases metabolism
Binding Sites drug effects
Dihydroxyacetone Phosphate chemistry
Dose-Response Relationship, Drug
Enzyme Inhibitors chemistry
Escherichia coli Proteins metabolism
Iron-Sulfur Proteins metabolism
Models, Molecular
Molecular Structure
Structure-Activity Relationship
Alkyl and Aryl Transferases antagonists & inhibitors
Dihydroxyacetone Phosphate pharmacology
Enzyme Inhibitors pharmacology
Escherichia coli Proteins antagonists & inhibitors
Iron-Sulfur Proteins antagonists & inhibitors
Subjects
Details
- Language :
- English
- ISSN :
- 1521-3773
- Volume :
- 51
- Issue :
- 31
- Database :
- MEDLINE
- Journal :
- Angewandte Chemie (International ed. in English)
- Publication Type :
- Academic Journal
- Accession number :
- 22715136
- Full Text :
- https://doi.org/10.1002/anie.201202261