Antibacterial Target DXP Synthase Catalyzes the Cleavage of d-Xylulose 5-Phosphate: a Study of Ketose Phosphate Binding and Ketol Transfer Reaction
Author:
Affiliation:
1. Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, United States
Funder
National Institute of Allergy and Infectious Diseases
Johns Hopkins University
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.2c00274
Reference94 articles.
1. Cloning and characterization of a gene from Escherichia coli encoding a transketolase-like enzyme that catalyzes the synthesis of D-1-deoxyxylulose 5-phosphate, a common precursor for isoprenoid, thiamin, and pyridoxol biosynthesis
2. Identification of a thiamin-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-D-xylulose 5-phosphate precursor to isoprenoids, thiamin, and pyridoxol
3. Glyceraldehyde 3-Phosphate and Pyruvate as Precursors of Isoprenic Units in an Alternative Non-mevalonate Pathway for Terpenoid Biosynthesis
4. DXS as a target for structure-based drug design
5. Druggability of the enzymes of the non-mevalonate-pathway
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1. An activity-based probe for antimicrobial target DXP synthase, a thiamin diphosphate-dependent enzyme;Frontiers in Chemical Biology;2024-05-07
2. Potent Inhibition of E. coli DXP Synthase by a gem-Diaryl Bisubstrate Analog;ACS Infectious Diseases;2024-03-21
3. Disruption of an Active Site Network Leads to Activation of C2α-Lactylthiamin Diphosphate on the Antibacterial Target 1-Deoxy-d-xylulose-5-phosphate Synthase;Biochemistry;2024-02-23
4. Design of thiamine analogues for inhibition of thiamine diphosphate (ThDP)-dependent enzymes: Systematic investigation through Scaffold-Hopping and C2-Functionalisation;Bioorganic Chemistry;2023-09
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