Dr. Henry C. Reeves

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The major metabolic route for the synthesis of phosphoenolpyruvate is from 2-phosphoglycerate catalyzed by the enzyme enolase (EC 4.2.1.11). Enolase occurs at the converging point between glycolysis and gluconeogenesis and may be an important regulatory enzyme. Growth ofEscherichia coli JA 200 pLC 11-8 to stationary phase in low-phosphate medium(More)
The NADP+-specific glutamate dehydrogenase (GDH) fromEscherichia coli strain D5H3G7, an enzyme that catalyzes the interconversion of α-ketoglutarate andl-glutamate, has been shown to be phosphorylated in vitro in an ATP-dependent enzymatic reaction. The phosphorylated protein is extremely acid labile and is unstable at high pH. Treatment of GDH with diethyl(More)
Isocitrate lyase has been purified to homogeneity, as determined by SDS-polyacrylamide gel electrophoresis and subsequent silver staining, fromEscherichia coli D5H3G7. The enzyme was found to have a subunit molecular weight of 48,000 and a native molecular weight of 188,000 as determined by gel filtration chromatography. Thus, the enzyme appears to have(More)
A method for the purification of enolase (EC 4.2.1.11) from an overproducing strain ofEscherichia coli JA 200 pLC 11–8 is described. The procedure included treatment of the crude sonic extract with protamine sulfate, followed by ammonium sulfate fractionation, hydrophobic interaction chromatography with phenyl Sepharose, HPLC ion exchange chromatography(More)
The NADP+-specific glutamate dehydrogenase fromEscherichia coli has been purified to electrophoretic homogeneity. The enzyme was purified 40-fold and has a specific activity of 23. Glutamate dehydrogenase fromE. coli is a hexameric enzyme with a native molecular weight of 275 KDa composed of monomers each with a molecular weight of 44.5 KDa. In(More)
Properties of isocitrate lyase fromEscherichia coli, the first enzyme of the glyoxylate bypass, have been compared from cells grown on either acetate or glycolate as the sole carbon source. Michaelis constants for isocitrate, isoelectric points, native and subunit molecular weights, antigenic properties, peptide mapping with V-8 or trypsin, and several(More)
Glutamate dehydrogenase fromEscherichia coli is phosphorylated in vitro in an ATP-dependent enzymatic reaction. The phosphorylated protein, when exposed to acid conditions, releases the phosphate; this implies that the phosphorylation site is not on a serine, tyrosine, or threonine residue(s). Treatment of glutamate dehydrogenase with diethyl pyrocarbonate,(More)
Several lines of evidence indicate that the in vivo phosphorylation of isocitrate dehydrogenase (EC 1.1.1.42) inEscherichia coli occurs at multiple sites: first, the phosphorylated enzyme can be resolved by two-dimensional electrophoresis into three distinct spots differing in charge; second, the analysis of its phosphoamino acid content shows that it is(More)
The in vitro phosphorylation of isocitrate lyase was demonstrated in partially purified sonic extracts ofEscherichia coli. Extracts were incubated with [gamma32P]-ATP and subsequently analyzed by two-dimensional polyacrylamide gel electrophoresis. Isocitrate lyase was determined to be phosphorylated by autoradiography and Western blot analyses of the gels.(More)
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