Disruption of an Active Site Network Leads to Activation of C2α-Lactylthiamin Diphosphate on the Antibacterial Target 1-Deoxy-<scp>d</scp>-xylulose-5-phosphate Synthase-Reference-Cited by-同舟云学术

Disruption of an Active Site Network Leads to Activation of C2α-Lactylthiamin Diphosphate on the Antibacterial Target 1-Deoxy-d-xylulose-5-phosphate Synthase

Published:2024-02-23 Issue:5 Volume:63 Page:671-687
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Toci Eucolona M.¹^ORCID,Austin Steven L.²,Majumdar Ananya³,Woodcock H. Lee²^ORCID,Freel Meyers Caren L.¹^ORCID

Affiliation:

1. Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, United States

2. Department of Chemistry, University of South Florida, Tampa, Florida 33620, United States

3. Biomolecular NMR Center, Johns Hopkins University, Baltimore, Maryland 21218, United States

Funder

National Institute of Allergy and Infectious Diseases

National Institutes of Health

Pittsburgh Supercomputing Center

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.3c00735

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. Thiamin (Vitamin B1) Biosynthesis and Regulation: A Rich Source of Antimicrobial Drug Targets?

4. X-ray crystallography–based structural elucidation of enzyme-bound intermediates along the 1-deoxy-d-xylulose 5-phosphate synthase reaction coordinate

5. DXS as a target for structure-based drug design

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