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University of Illinois at Urbana-Champaign

A Study of the Mechanistic Diversity Inherent to the Ribulose Phosphate Binding Barrel Superfamily

Abstract

dc:description

To probe the functional plasticity of the RPBB superfamily, rational design was used to enhance the UPS activity within the KGPDC scaffold. The triple mutant E112D/T169A/R139V had an enhancement in kcat /KM by 260 fold over wild-type KGPDC. Structural studies suggest that little perturbation of the active site occurs with the 3 mutations.

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
  • Akana, Julie A.
Contributors dc:contributor
  • Gerlt, John A.

Subjects

dc:subject × 1

Rights

Language dc:language
eng

Identifiers

dc:identifier.*
Identifier
(MiAaPQ)AAI3223532
OAI identifier oai:identifier
oai:www.ideals.illinois.edu:2142/84822

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

Akana, Julie A.. A Study of the Mechanistic Diversity Inherent to the Ribulose Phosphate Binding Barrel Superfamily. Dissertation thesis, University of Illinois at Urbana-Champaign, 2015. http://hdl.handle.net/2142/84822