Open Access. Powered by Scholars. Published by Universities.®
- Publication
Articles 1 - 2 of 2
Full-Text Articles in Life Sciences
Allosteric Regulation Of Pyruvate Carboxylase, Yumeng Liu
Allosteric Regulation Of Pyruvate Carboxylase, Yumeng Liu
Dissertations (1934 -)
Pyruvate carboxylase (PC; E.C.6.4.1.1) is a multifunctional, biotin-dependent enzyme that catalyzes the MgATP-dependent carboxylation of pyruvate to oxaloacetate. The overall reaction is accomplished by the coupling of two half reactions occurring at two spatially distinct catalytic domains by the translocation of a carrier domain, resulting in a net transfer of CO2 from bicarbonate to pyruvate. PC activity is regulated by multiple allosteric effectors with acetyl CoA serving as an activator in most species and L-aspartate serving as an inhibitor for microbial PC. The kinetic characterization of PC from different species have revealed that PC homologs are subject to divergent degrees …
Studies Into The Allosteric Regulation Of Adp-Glucose Pyrophosphorylases, Benjamin Luke Hill
Studies Into The Allosteric Regulation Of Adp-Glucose Pyrophosphorylases, Benjamin Luke Hill
Dissertations
The synthesis of glycogen in bacteria and starch in plants is allosterically controlled by the production of ADP-glucose by ADP-glucose pyrophosphorylase. Using computational studies, site directed mutagenesis, and kinetic characterization, and protein crystallography we found a critical region for transmitting the allosteric signal in the Escherichia coli and A. tumefaciens ADP-glucose pyrophosphorylase. Molecular dynamics simulations and structural comparisons with other ADP-glucose pyrophosphorylases provided information to hypothesize communication pathways that link allosteric and active sites, and this was tested by site-directed mutagenesis and kinetic characterization of the mutant enzymes. In addition, the application of x-ray crystallography enabled the pinpointing of the …