Jack Preiss
University Distinguished Professor

• B.S. 1953,City College of New York
• Ph.D. 1957,Duke University.
• Postdoctoral Fellow,1956-58,Duke Univ.
• Postdoctoral Fellow,1958-59, Washington Univ., St. Louis
• Postdoctoral Fellow,1959-60, Stanford School of Medicine
• Scientist,1960-62,National Institutes of Health.
• Faculty Member,1962-84, Univ of Calif. - Davis.
• Guggenheim Memorial Fellowship,1969-70.
• Charles Pfizer Award,1971,American Chemical Society.
• Alexander Von Humboldt Senior U.S. Scientist Award,1984.
• Chair, MSU Biochemistry,1985-89.
• Alsberg-Schoch Memorial,1990,American Assoc. of Cereal Chemists.
• Japanese Society of Starch Science Merit Award,1992.
• Distinguished Faculty Award,1994,MSU.
• Distinguished Faculty Award,1996,CNS Alumni Assoc.
• Distinguished Faculty Award,1997, Mich. Assoc. of Governing Boards.
• Loomis Lecturer,1998,Iowa State University.
• University Distinguished Professor,2001, MSU.
• Highly Cited Researcher,January 2004,ISI (isihighlycited.com)
• Fellow, American Association for the Advancement of Science, 2007
• Elected Fellow of the American Society of Plant Biology, 2008

preiss@msu.edu
309 Biochemistry
Michigan State University
East Lansing, MI 48824-1319
Office:517-353-3137
Lab:353-3247

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Jack Preiss

Research Interests

Plants and bacteria use similar reactions to synthesize the major carbohydrate reserve polymers, starch and glycogen. First, ADP-glucose (ADPG) is synthesized from ATP and glucose-1-P via catalysis by ADPG pyrophosphorylase. The glycosyl portion of the sugar nucleotide is then transferred to the non-reducing end of a growing glucose polymer chain to form new 1,4-glucosyl linkages. The synthesis of the 1,6-glucosidic linkage is catalyzed by branching enzyme. Regulation of starch and glycogen synthesis occurs via allosteric regulation of the ADPG pyrophosphorylase-catalyzed reaction. Glycolytic intermediates are activators and either AMP, ADP or Pi are inhibitors. Another regulatory facet observed is the derepression of the glycogen biosynthetic levels in the bacteria when the exponential phase of growth shifts into stationary phase. In maize and other plants, similar observations have been made in the endosperm. The levels of the starch biosynthetic enzymes dramatically increase in the later stages of development.

The glycolytic intermediate activators of the ADPG pyrophosphorylase vary for many of the systems studied, and a rough correlation has been seen with respect to the nature of the activator and the major carbon assimilation pathway in the organism. For example, the activator for the higher plant ADPG pyrophosphorylases is 3-phosphoglycerate and the major activator for the ADPG pyrophosphorylase of the bacteria that utilize glycolysis as their major catabolic pathway is fructose-1,6-P2. Thus, it is of great interest to determine and compare the structure and function of the catalytic and effector sites of the bacterial and plant ADPG pyrophosphorylases. MORE

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