|Statement||by Theodore Roger Allen.|
|Contributions||Boston College. Dept. of Biology.|
|The Physical Object|
|Pagination||vi, 81 leaves :|
|Number of Pages||81|
The purification and properties of formate dehydrogenase and nitrate reductase from Escherichia coli. Enoch HG, Lester RL. The membrane-bound formate dehydrogenase of Escherichia coli grown anaerobically in the presence of nitrate was solubilized with deoxycholate and purified to near by: Escherichia coli was grown under various culture conditions. Variations in the levels of formate dehydrogenase which reacts with methylene blue (MB) or phenazine methosulfate (PMS) (N enzyme), formate dehydrogenase which reacts with benzyl viologen (BV) (H enzyme), formate oxidase and hydrogenlyase were analyzed. It was observed that formate Cited by: Kinetics of formate dehydrogenase of Escherichia coli formate-hydrogenlyase Article (PDF Available) in Journal of Biological Chemistry (21) August with 50 Reads. Metabolic engineering of Escherichia coli: increase of NADH availability by overexpressing an NAD(+)-dependent formate dehydrogenase. Berríos-Rivera SJ(1), Bennett GN, San KY. Author information: (1)Department of Bioengineering and Chemical Engineering, Rice University, Houston, Texas, by:
Mutants of Escherichia coli Specifically Deficient in Respiratory Formate Dehydrogenase Activity Article (PDF Available) in Journal of general microbiology (12) . Abstract. The lipoamide dehydrogenase gene (lpdA) encoding the E3 subunits of both the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes of Escherichia coli, is expressed from the upstream pdh and internal lpd promoters of the pdh operon (pdhR-aceEF-lpdA).Under aerobic conditions, the specific components of the 2-oxoglutarate Cited by: Inhibition of formate dehydrogenase activities The results of exposure of the two enzymes to potential inhibitors or inhibitory procedures are Table 3 Effect of inhibitors on formate dehydrogenase of E. coli The soluble fraction prepared from anaerobically grown E. coli was further fractionated by centrifugation through a sucrose gradient Cited by: Xylonate is a valuable chemical for versatile applications. Although the chemical synthesis route and microbial conversion pathway were established decades ago, no commercial production of xylonate has been obtained so far. In this study, the industrially important microorganism Escherichia coli was engineered to produce xylonate from xylose. Through the coexpression .
Acta, I22 (I) BBA Regulation of pyruvate dehydrogenase activity in Escherichia coil KI2 The synthesis of the pyruvate dehydrogenase complex (pyruvate dehydro- genase, EC plus lipoate acetyltransferase, EC plus lipoamide dehy- drogenase, EC ) in Escherichia coli KI~2 has been proposed to be by: Background: d-Malate dehydrogenase (DmlA) is involved in d-malate catabolism in Escherichia coli. Results: When expressed in the presence of d-malate, DmlA allows growth of a ΔleuB strain without leucine. Conclusion: DmlA physiologically contributes to two core metabolic reactions. Significance: Several high level activities may coexist in one enzyme and be . Abstract. l-Cysteine desulfurases provide sulfur to several metabolic pathways in the form of persulfides on specific cysteine residues of an acceptor protein for the eventual incorporation of sulfur into an end is one of the three Escherichia coli l-cysteine interacts with FdhD, a protein essential for the activity of formate . E. coli performs mix-acid fermentation when grown anaerobically with acetate, ethanol, lactate, formate and succinate as major products. During fermentation, NADH produced in catabolic process is used to produce fermentation products to regenerate NAD, meanwhile net ATP is produced in the process to sustain cell growth [ 22 ].Cited by: 6.