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• W1603661711 abstract "Control of Pyrimidine Biosynthesis in Escherichia coli by a Feed-back Mechanism (Yates, R. A., and Pardee, A. B. (1956) J. Biol. Chem. 221, 757–770) The Enzymology of Control by Feedback Inhibition (Gerhart, J. C., and Pardee, A. B. (1962) J. Biol. Chem. 237, 891–896) Arthur B. Pardee began his scientific training as an undergraduate at the University of California, Berkeley where he earned a Bachelor of Science degree in 1942. He then went on to the California Institute of Technology to do his Ph.D. with Linus Pauling, performing some of the first studies with purified antibodies. After earning his Ph.D. in 1947, Pardee took a Merck postdoctoral fellowship with Van Potter at the University of Wisconsin. Because his mother had died of cancer in 1942, Pardee was interested in doing what he could to contribute to cancer research. At Wisconsin, Pardee studied the deregulation of oxidative phosphorylation and the Krebs cycle in cancers using tissue homogenates. In 1949 Pardee joined the faculty of the biochemistry department and the virus laboratory at the University of California, Berkeley. There he discovered the ribonucleoprotein particles in bacteria that were later named ribosomes as well as the photosynthetic particles that were named chromatophores. Wanting to learn whether virus infection alters host metabolism, he discovered that nine enzyme activities changed after Escherichia coli was infected with bacteriophage. During the 1950s, when biochemists were busy creating a map of metabolism without regard to metabolic regulation, investigators became interested in how bacteria were able to produce just the right amount of components necessary for growth and responded to the addition of growth factors in the medium. Earlier, several indications of metabolic control had been reported (1Roberts R.B. Abelson P.H. Cowie D.B. Bolton E.T. Britten R.J. Studies of biosynthesis in Escherichia coli..Carnegie Inst. Wash. Publ. 1955; 607Google Scholar, 2Koch A.L. Putnam F.W. Evans E.A. The purine metabolism of Escherichia coli..J. Biol. Chem. 1952; 197: 105-112Abstract Full Text PDF PubMed Google Scholar, 3Abelson P.H. Bolton E.T. Aldous E. Utilization of carbon dioxide in the synthesis of proteins by Escherichia coli. II..J. Biol. Chem. 1952; 198: 173-178Abstract Full Text PDF PubMed Google Scholar, 4Gots J.S. Chu E.C. Studies on purine metabolism in bacteria. I. The role of p-aminobenzoic acid..J. Bacteriol. 1952; 64: 537-546Crossref PubMed Google Scholar, 5Love S.H. Gots J.S. Purine metabolism in bacteria. III. Accumulation of a new pentose-containing arylamine by a purine-requiring mutant of Escherichia coli..J. Biol. Chem. 1955; 212: 647-654Abstract Full Text PDF PubMed Google Scholar, 6Brooke M.S. Ushiba D. Magasanik B. Some factors affecting the excretion of orotic acid by mutants of Aerobacter aerogenes..J. Bacteriol. 1954; 68: 534-540Crossref PubMed Google Scholar), and in 1953 Edward A. Adelberg and H. Edwin Umbarger reported the observation that the presence of valine in the growth medium of E. coli inhibited the formation of α-ketoisovalerate, a valine precursor, and noted that this was likely a general control phenomenon, although the mechanism was unclear (7Adelberg E.A. Umbarger H.E. Isoleucine and valine metabolism in Escherichia coli.V. α-Ketoisovaleric acid accumulation..J. Biol. Chem. 1953; 205: 475-482Abstract Full Text PDF PubMed Google Scholar). In 1956, Umbarger reported negative feedback by isoleucine on threonine deaminase, the first enzyme in the biosynthesis of isoleucine (8Umbarger H.E. Evidence for a negative-feedback mechanism in the biosynthesis of isoleucine..Science. 1956; 123: 848Crossref PubMed Scopus (205) Google Scholar). Umbarger's role in the description of feedback inhibition will be the subject of a future Journal of Biological Chemistry (JBC) Classic. Pardee, along with Richard Yates, described a general control mechanism for the pyrimidine pathway. This is the subject of the first JBC Classic reprinted here. Using pyrimidine-requiring mutants of E. coli, Pardee and Yates noted that the presence of uracil inhibited the formation of pyrimidine intermediates earlier than orotic acid (9Yates R.A. Pardee A.B. Pyrimidine biosynthesis in Escherichia coli..J. Biol. Chem. 1956; 221: 743-756Abstract Full Text PDF PubMed Google Scholar). Pardee and Yates then undertook additional in vivo and in vitro studies on E. coli pyrimidine-requiring mutants, which confirmed their initial observations. From these experiments, Pardee concluded that the end product of a biosynthetic pathway can be an inhibitor of its initial enzymatic reaction. However, the molecular mechanism of feedback inhibition created a problem. At that time, it was generally thought that inhibitors compete with substrates for binding to the active site of the enzyme. Yet, end products and substrates often differed greatly in size, shape, and charge, so how could they compete for a site specific for the substrate, which would not be suited for binding the end product? This is the subject of the second JBC Classic reprinted here. Pardee and John Gerhart approached this problem using aspartate transcarbamylase, an enzyme known to be inhibited by a nucleotide end product, which competes with a structurally unrelated substrate, an amino acid. They discovered that the enzyme was inhibited by cytidine triphosphate and that this inhibition was reversed by high concentrations of its substrate, aspartate. Because cytidine triphosphate had no structural similarity to aspartate, Pardee concluded that there must be a regulatory site distinct from the active site. This was confirmed by the observation that ATP activates aspartate transcarbamylase. ATP, which is not a substrate, could not bind to the active site because this would be inhibitory, thus it must bind to a different, regulatory site. Gerhart went on to separate the regulatory and catalytic subunits of aspartate transcarbamylase. Currently, Gerhart is an emeritus professor in the Department of Molecular and Cell Biology at the University of California, Berkeley, studying the early development of the amphibian Xenopus laevis. He has received several awards and honors for his research including the American Society for Cell Biology's E. B. Wilson Award (1997) and election to the National Academy of Sciences (1990). After his studies on feedback inhibition, Pardee turned to the regulation of enzyme expression by repression, and his work became the basis for current concepts of the major mechanism for regulating gene expression in both prokaryotes and eukaryotes. Pardee moved to Princeton to become the first Chairman of the Biochemical Sciences Department in 1961. There, he began to investigate the differences between cancer cells and normal cells, including changes in transport and carbohydrates on the cell surfaces. He also studied the disregulation of the cell cycle in cancer and discovered that regulation for normal cells is exerted in late G1 phase and that the restriction point requirements are relaxed in cancer cells, providing a basis for the greater proliferative capacity of cancer. In 1975 Pardee moved to the Dana-Farber Cancer Institute and Harvard University. He served as Chief for the Division of Cell Growth and Regulation at the Dana-Farber Cancer Institute and became an emeritus professor in 1992. His current work focuses on finding methods for detecting cancer earlier and searching for novel agents to treat cancer more effectively. He and Peng Liang are credited with the discovery of the differential display technique, which is widely used in examining the activation of genes in cells. Pardee was elected to the National Academy of Sciences, the Institute of Medicine, and the American Academy of Arts and Sciences. He has served as president of the American Society for Biochemistry and Molecular Biology and the American Association for Cancer Research. More information on Pardee's research can be found in his JBC Reflections (10Pardee A.B. Regulation, restriction, and reminiscences..J. Biol. Chem. 2002; 277: 26709-26716Abstract Full Text Full Text PDF PubMed Scopus (8) Google Scholar)." @default.
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• W1603661711 title "The Enzymology of Feedback Inhibition by Arthur B. Pardee" @default.
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