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Title:Essential Fatty Acid Biosynthetic Enzymes of Escherichia Coli and Lactococcus Lactis Subsp. Lactis
Author(s):Lai, Chiou-Yan
Doctoral Committee Chair(s):Cronan, John E., Jr
Department / Program:Microbiology
Degree Granting Institution:University of Illinois at Urbana-Champaign
Subject(s):Chemistry, Biochemistry
Abstract:FabG, beta-ketoacyl-ACP reductase, performs the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to the beta-hydroxyacyl-ACP products. I report the first characterized fabG mutants. By chemical mutagenesis followed by a tritium suicide procedure, I obtained three conditionally-lethal temperature-sensitive fabG (fabGts) mutants. The E. coli mutant has two point mutations: A154T and E233K. In Salmonella enterica Serovar Typhimurium fabGts mutants one strain had a point mutation, S224F whereas the second strain contained two mutations (M125I and A223T). All of the altered residues of the FabG mutant proteins are located on or near the two-fold axes of symmetry at the dimer interfaces in this homotetrameric protein suggesting that the quanternary structures of the mutant FabG proteins may be disrupted at the nonpermissive temperature.
Issue Date:2003
Description:143 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2003.
Other Identifier(s):(MiAaPQ)AAI3101892
Date Available in IDEALS:2015-09-28
Date Deposited:2003

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