Ethanologenic Enzymes of Zymomonas mobilis
Author(s) -
L. O. Ingram
Publication year - 1999
Publication title -
osti oai (u.s. department of energy office of scientific and technical information)
Language(s) - English
Resource type - Reports
DOI - 10.2172/7217
Subject(s) - zymomonas mobilis , glycolysis , biochemistry , aldolase a , metabolic pathway , flux (metallurgy) , enzyme , biology , fermentation , chemistry , ethanol fuel , organic chemistry
Zymomonas mobilis is a unique microorganism in being both obligately fermentative and utilizing a Entner-Doudoroff pathway for glycolysis. Glycolytic flux in this organism is readily measured as evolved carbon dioxide, ethanol, or glucose consumed and exceeds 1 {micro}mole glucose/min per mg cell protein. To support this rapid glycolysis, approximately 50% of cytoplasmic protein is devoted to the 13 glycolytic and fermentative enzymes which constitute this central catabolic pathway. Only 1 ATP (net) is produced from each glucose metabolized. During the past grant period, we have completed the characterization of 11 of the 13 glycolytic genes from Z. mobilis together with complementary but separate DOE-fimded research by a former post-dot and collaborator, Dr. Tyrrell Conway. Research funded in my lab by DOE, Division of Energy Biosciences can be divided into three sections: A. Fundamental studies; B. Applied studies and utility; and C. Miscellaneous investigations
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