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David M. Chipman

Researcher at Ben-Gurion University of the Negev

Publications -  100
Citations -  4402

David M. Chipman is an academic researcher from Ben-Gurion University of the Negev. The author has contributed to research in topics: Active site & Protein subunit. The author has an hindex of 34, co-authored 100 publications receiving 4255 citations. Previous affiliations of David M. Chipman include Northeastern University & Weizmann Institute of Science.

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Models for nicotinamide coenzymes. Isotope effect discrepancies in the reaction of dihydronicotinamides with trifluoroacetophenone are due to adduct formation

TL;DR: In this article, the authors measured isotope effects during oxidation-reduction reactions of two dihydronicotinamides and explained the kinetics of the redox reaction by a simple hydride transfer.
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Role of a conserved arginine in the mechanism of acetohydroxyacid synthase: catalysis of condensation with a specific ketoacid substrate.

TL;DR: Engel et al. as mentioned in this paper showed that mutagenesis of arginine residue in Escherichia coli AHAS isozyme II (Arg276) confirms that it is required for rapid and specific reaction of the second ketoacid substrate.
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Acetohydroxyacid synthase from Mycobacterium avium and its inhibition by sulfonylureas and imidazolinones

TL;DR: The relative potency of the different inhibitors towards the M. avium enzyme was unlike their potency towards other AHASs whose inhibitor profile has been reported, emphasising the advantage of using a mycobacterial enzyme as a tool in the search for new anti-TB drugs.
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The carboligation reaction of acetohydroxyacid synthase II: Steady-state intermediate distributions in wild type and mutants by NMR

TL;DR: Detailed NMR analysis was used to determine microscopic rate constants for elementary steps in the reactions of AHAS II and mutants altered at conserved residues Arg-276, Trp-464, and Met-250 to speculate that the specificity of carboligation and product liberation may be cumulative if the former is not completely committed.
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Enhanced production of acetoin and butanediol in recombinant Enterobacter aerogenes carrying Vitreoscilla hemoglobin gene.

TL;DR: This vgb/VHb related effect appears to be due to an increase of flux through the acetoin/butanediol pathway, but not at the expense of acid production.