Pre-Steady-State Kinetic Analysis of 1-Deoxy-d-xylulose-5-phosphate Reductoisomerase from Mycobacterium tuberculosis Reveals Partially Rate-Limiting Product Release by Parallel Pathways
Author:
Affiliation:
1. Department of Chemistry, University at Buffalo, The State University of New York, Buffalo, New York 14260, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi300513r
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4. 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
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3. The Role of Phosphate in a Multistep Enzymatic Reaction: Reactions of the Substrate and Intermediate in Pieces;Journal of the American Chemical Society;2015-02-10
4. Mechanism and inhibition of 1-deoxy-d-xylulose-5-phosphate reductoisomerase;Bioorganic Chemistry;2014-12
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