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Showing 1 to 7 of 7 for “"phosphite dehydrogenase"”.
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Mechanistic Studies and Synthetic Applications of Phosphite Dehydrogenase
Cytochrome c oxidase, an enzyme that catalyzes the reduction of oxygen to water, has a binuclear center as well as a unique post-translational modification in the active site. Specifically, there is a crosslink between the nitrogen (Nepsilon2) of His240 and the carbon (Cepsilon 2) of Tyr244 …
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Kinetic Analysis and pH Dependence of the Phosphite Dehydrogenase Reaction
The pH-rate profiles for active site mutants Lys76Ala, Glu266G1n, and Arg237Lys are also bell-shaped and the higher pKa of each is 8.4, which is also consistent with that observed for the pH dependence of sulfite inhibition for the wild type enzyme. Interestingly, the acidic limb of the Glu266Gln …
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Directed Evolution of Phosphite Dehydrogenase and Engineered Biosynthesis of Fr-900098
Another area in which biocatalysts are increasingly being used is in the production of small secondary metabolites, particularly antibiotics. Phosphonates are a small but growing class of compounds with many useful therapeutic properties. In particular, the phosphonates fosmidomycin and FR-900098 …
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Understanding, Optimization, and Application of Phosphite Dehydrogenase: Advancing NAD(P)H Regeneration
NAD(P)H regeneration is an industrially important process that supports biocatalytic reactions that utilize these cofactors. PTDH shows promise for NAD(P)H regeneration and was therefore optimized for industrial application. The cofactor specificity of PTDH was relaxed by rational design using the …
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Mechanistic studies to determine the catalytic roles of active site residues in phosphite dehydrogenase
Phosphite dehydrogenase (PTDH) catalyzes the oxidation of phosphite to phosphate with the concurrent reduction of NAD+ to NADH. The mechanism of the reaction resembles a phosphoryl transfer reaction. A nucleophilic displacement reaction occurs on the phosphoryl group, with water or hydroxide …
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Use of solution-state nuclear magnetic resonance spectroscopy to determine the structures of medicinally relevant peptides and proteins
… to the producing organism. The final system was phosphite dehydrogenase, an enzyme putatively useful in the regeneration of nicotinamide cofactors. By studying these systems, it is believed that advances could be made toward novel antibiotic compounds to alleviate the increasing pressure of …
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Engineering of an efficient and enantioselective biocatalyst for the preparation of chiral pharmaceutical intermediates
… was developed by co-expressing a glucose dehydrogenase from Bacillus substilis or a phosphite dehydrogenase from Pseudomonas stutzeri together with the P450pyr system in a recombinant Escherichia coli.