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• W2022837084 abstract "1‐Deoxy‐ d ‐xylulose 5‐phosphate ( DXP ) synthase catalyzes the formation of DXP from pyruvate and d ‐glyceraldehyde 3‐phosphate (Gra P ) in a thiamin diphosphate‐dependent manner, and is the first step in the essential pathway to isoprenoids in human pathogens. Understanding the mechanism of this unique enzyme is critical for developing new anti‐infective agents that selectively target isoprenoid biosynthesis. The present study used mutagenesis and a combination of protein fluorescence, CD and kinetics experiments to investigate the roles of Arg420, Arg478 and Tyr392 in substrate binding and catalysis. The results support a random sequential, preferred order mechanism, and predict that Arg420 and Arg478 are involved in binding of the acceptor substrate, Gra P . d ‐Glyceraldehyde, an alternative acceptor substrate lacking the phosphoryl group predicted to interact with Arg420 and Arg478, also accelerates decarboxylation of the predecarboxylation intermediate C2α‐lactylthiamin diphosphate ( LT h DP ) on DXP synthase, indicating that this binding interaction is not absolutely required, and that the hydroxyaldehyde sufficiently triggers decarboxylation. Unexpectedly, Tyr392 contributes to Gra P affinity, and is not required for LT h DP formation or its Gra P ‐promoted decarboxylation. Time‐resolved CD spectroscopy and NMR experiments indicate that LT h DP is significantly stabilized on R420A and Y392F variants as compared with wild‐type DXP synthase in the absence of acceptor substrate, but these substitutions do not appear to affect the rate of Gra P ‐promoted LT h DP decarboxylation in the presence of high levels of Gra P , and LT h DP formation remains the rate‐limiting step. These results suggest a role of these residues in promoting Gra P binding, which in turn facilitates decarboxylation, and also highlight interesting differences between DXP synthase and other thiamin diphosphate‐dependent enzymes." @default.
• W2022837084 created "2016-06-24" @default.
• W2022837084 creator A5009378425 @default.
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• W2022837084 date "2014-05-12" @default.
• W2022837084 modified "2023-10-13" @default.
• W2022837084 title "Defining critical residues for substrate binding to 1‐deoxy‐<scp>d</scp>‐xylulose 5‐phosphate synthase – active site substitutions stabilize the predecarboxylation intermediate C2α‐lactylthiamin diphosphate" @default.
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• W2022837084 doi "https://doi.org/10.1111/febs.12823" @default.
• W2022837084 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4065394" @default.
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