BIOSYNTHESIS OF SERINE IN ESCHERICHIA COLI AND SALMONELLA TYPHIMURIUM

Abstract

Umbarger, H. E. (Long Island Biological Association, Cold Spring Harbor, N.Y.), Merle A. Umbarger, and Patrick M. L. Siu. Biosynthesis of serine in Escherichia coli and Salmonella typhimurium. J. Bacteriol. 85:1431–1439. 1963.—Evidence for the operation in extracts of Escherichia coli of a pathway from glucose to serine involving 3-phosphoglycerate, phosphohydroxypyruvate, and phosphoserine as intermediates was obtained by the technique of isotopic competition. The steps of the pathway were demonstrated in extracts of E. coli and Salmonella typhimurium. The first reaction was studied in the reverse of the biosynthetic direction by observing the disappearance of reduced nicotinamide adenine dinucleotide in the presence of phosphohydroxypyruvate. The enzyme catalyzing this reaction was missing in two E. coli mutants that required serine or glycine for growth and in a representative of one of two genetically distinct classes of S. typhimurium serine-glycine auxotrophs. The second reaction, the amination of phosphohydroxypyruvate, was also studied in the reverse of the biosynthetic direction using α-ketoglutarate as the amino acceptor in a transamination reaction with phosphoserine. The final step, the cleavage of phosphoserine, could not be catalyzed by extracts prepared from cells of S. typhimurium serine-glycine auxotrophs of the second genetic class. It has been concluded that these three reactions provide the only significant pathway to serine in these organisms.