Characterization of the Escherichia Coli Acyl Carrier Protein Phosphodiesterase

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.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Microbiology

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Thomas, Jacob

Contributors dc:contributor

• Cronan, John E., Jr

• Biology, Microbiology

Language dc:language

eng

Identifier

(MiAaPQ)AAI3395514

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/86713