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University of Illinois at Urbana-Champaign

PaaG and PaaF: New Members of the Crotonase Superfamily

Abstract

dc:description

Using the published operon structure of phenylacetate utilization, BLAST searches of public sequence databases, and metabolic information from a related compound, two pathways for phenylacetate metabolism were proposed. The genes encoding PaaF, PaaG, PaaH, PaaJ, and PaaI were cloned, and the proteins expressed, and purified. I showed by enzyme assays using purified proteins that beta-oxidation in phenylacetate metabolism proceeds via adipyl-CoA intermediates. I showed that PaaG catalyzes the isomerization of trans-Delta 3-hexenedioyl-CoA to trans-Delta2-hexenedioyl-CoA, uses an Asp as a general base, and the reaction proceeds without incorporation of solvent protons.

Degree

thesis:*
Name thesis:degree_name
Ph.D.
Level thesis:degree_level
Dissertation
Discipline thesis:degree_discipline
Biochemistry
Grantor
University of Illinois at Urbana-Champaign
Year dc:date
2015

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Lies, Mark Andrew, III
Contributors dc:contributor
  • Gerlt, John A.

Subjects

dc:subject × 1

Rights

Language dc:language
eng

Identifiers

dc:identifier.*
Identifier
(MiAaPQ)AAI3086121
OAI identifier oai:identifier
oai:www.ideals.illinois.edu:2142/84793

Chain of custody

source
Harvested from
University of Illinois - Urbana-Champaign
Base URL
www.ideals.illinois.edu/oai-pmh
Last updated
2026-07-22
Source record
OAI-PMH GetRecord
citation

Lies, Mark Andrew, III. PaaG and PaaF: New Members of the Crotonase Superfamily. Dissertation thesis, University of Illinois at Urbana-Champaign, 2015. http://hdl.handle.net/2142/84793