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Apo structure of Mycobacterium tuberculosis 1-deoxy-d-xylulose 5-phosphate synthase DXPS: Dynamics and implications for inhibitor design.
Biochem Biophys Res Commun
January 2025
Chemical and Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, 9713 AV, Groningen, the Netherlands. Electronic address:
The enzyme 1-deoxy-d-xylulose-5-phosphate synthase (DXPS) catalyses the first step of the MEP pathway, a key process for isoprenoid biosynthesis in bacteria that is absent in humans, making it a promising drug target. We present the structure of Mycobacterium tuberculosis DXPS in its apo form, obtained through a soaking method that removes thiamine diphosphate (ThDP) and metals from pre-formed crystals. The apo structure had three regions with absence of electron density near the active site that are unique to the apo form of the enzyme.
View Article and Find Full Text PDFBisubstrate Analog Inhibitors of DXP Synthase Show Species Specificity.
Biochemistry
January 2025
Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, United States.
1-Deoxy-d-xylulose 5-phosphate synthase (DXPS) is a unique thiamin diphosphate (ThDP)-dependent enzyme that catalyzes the formation of DXP, a branchpoint metabolite required for the biosynthesis of vitamins and isoprenoids in bacterial pathogens. DXPS has relaxed substrate specificity and utilizes a gated mechanism, equipping DXPS to sense and respond to diverse substrates. We speculate that pathogens utilize this distinct gated mechanism in different ways to support metabolic adaptation during infection.
View Article and Find Full Text PDFSynergistic role of Rubisco inhibitor release and degradation in photosynthesis.
New Phytol
December 2024
Plant Molecular Biology (Botany), Faculty of Biology, Ludwig-Maximilians University Munich, Martinsried, D-82152, Germany.
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) exhibits catalytic promiscuity, resulting in error-prone reactions and the formation of inhibitory sugar phosphates. Specifically, Xylulose-1,5-bisphosphate (XuBP) acts as an inhibitor by binding to the active site of Rubisco, thereby impairing its catalytic function. Thermolabile Rubisco activase (Rca) facilitates the release of such inhibitors, including XuBP, by remodelling Rubisco.
View Article and Find Full Text PDFNovel Differentially Expressed LncRNAs Regulate Artemisinin Biosynthesis in .
Life (Basel)
November 2024
Key Laboratory of Beijing for Identification and Safety Evaluation of Chinese Medicine, Institute of Chinese Materia Medica, China Academy of Chinese Medical Sciences, Beijing 100700, China.
Long non-coding RNAs (lncRNAs) are crucial in regulating secondary metabolite production in plants, but their role in artemisinin (ART) biosynthesis, a key anti-malarial compound from Artemisia annua, remains unclear. Here, by investigating high-artemisinin-producing (HAP) and lowartemisinin-producing (LAP) genotypes, we found that the final artemisinin content in is influenced by the quantity of the precursor compounds. We report on RNA deep sequencing in HAP and LAP genotypes.
View Article and Find Full Text PDFFunctional Identification and Regulatory Active Site Screening of the Gene of .
Plants (Basel)
September 2024
College of Life Sciences, Northeast Agricultural University, Harbin 150030, China.
(L.) Schott has anti-inflammatory and antioxidant properties, and terpenoids are important components of its active constituents. The methyl-D-erythritol 4-phosphate (MEP) pathway is one of the major pathways for the synthesis of terpene precursors in plants, and 1-deoxy-D-xylulose-5-phosphate synthase (DXS) is the first rate-limiting enzyme in this pathway.
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