4538-02-7Relevant academic research and scientific papers
Structure-activity relationships of tulipalines, tuliposides, and related compounds as inhibitors of MurA
Mendgen, Thomas,Scholz, Therese,Klein, Christian D.
supporting information; experimental part, p. 5757 - 5762 (2010/12/24)
The enzyme MurA performs an essential step in peptidoglycan biosynthesis and is therefore a target for the discovery of novel antibacterial compounds. We report here the inhibition of MurA by natural products from tulips (tulipalines and tuliposides), and the structure-activity relationships of various derivatives. The inhibition of MurA can be related to antibacterial activity, and MurA is probably one of the relevant molecular targets of the tulipaline derivatives. MurA inhibition by this class of compounds depends on the presence of the substrate UNAG, which indicates non-covalent suicide inhibition as observed previously for cnicin. With respect to selectivity, however, the reactivity against arbitrary sulfhydryl groups, such as in glutathione, could not yet be sufficiently separated from MurA inhibition in the present dataset.
Substrate and reaction intermediate mimics as inhibitors of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase
Walker, Scott R.,Cumming, Hemi,Parker, Emily J.
supporting information; experimental part, p. 3031 - 3035 (2011/02/25)
3-Deoxy-d-arabino-heptulosonate 7-phosphate (DAH7P) synthase catalyses the aldol-like addition of phosphoenolpyruvate (PEP) to d-erythrose 4-phosphate in the first step of the shikimate pathway to aromatic amino acids. A series of compounds, designed to m
