Characterization of the Escherichia Coli Acyl Carrier Protein Phosphodiesterase
Thomas, Jacob
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https://hdl.handle.net/2142/86713
Description
Title
Characterization of the Escherichia Coli Acyl Carrier Protein Phosphodiesterase
Author(s)
Thomas, Jacob
Issue Date
2009
Doctoral Committee Chair(s)
Cronan, John E., Jr
Department of Study
Microbiology
Discipline
Microbiology
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biology, Microbiology
Language
eng
Abstract
The activity of AcpH was also examined in relation to the toxicity of N-pentylpantothenamide, an analog of the CoA precursor pantothenic acid. This analog is known to be a substrate for three CoA synthetic enzymes, resulting in a CoA analog with a metabolically inactive prosthetic group (ethyldethia-CoA) which is then transferred to ACP. It was thought that ethyldethia-ACP carrying this inactive prosthetic group was a poor substrate for AcpH, resulting in the selective turnover of holo-ACP. I have shown that this is not the case: ethyldethia-ACP is a substrate for AcpH and overexpression of this enzyme results in increased resistance to N-pentylpantothenamide. I have also shown that CoA synthesis is inhibited upon treatment with the analog and this is likely to be a major cause of its growth-inhibitory effect.
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