I: Structure-function relationship of human phosphoglucose isomerase – A study bases on inherited mutations and GTP-bindingII: Functional analysis of the conserved histidine residue of Bamboo mosaic virus capping enzyme in the activity for the covalent [Enzyme-m7GMP] intermediate formation

• Main Authors: Hua-Yang Lin, 林華洋
• Other Authors: 孟孟孝
• Format: Others
• Language: en_US
• Published: 2012
• Online Access: http://ndltd.ncl.edu.tw/handle/t7ugsn

博士 === 國立中興大學 === 生物科技學研究所 === 100 === The part I in this dissertation is “Structure-function relationship of human phosphoglucose isomerase − A study bases on inherited mutations and GTP-binding”. This part contains two chapters. Chapter I entitled “Effects of inherited mutations on catalytic activity and structural stability of human phosphoglucose isomerase expressed in Escherichia coli” demonstrates the effects of the inherited mutations associated with nonspherocytic hemolytic anemia on the protein properties including kinetic parameter and protein stability. Chapter II entitled “Characterization of the novel binding of GTP to human phosphoglucose isomerase/autocrine motility factor” explicates a novel binding between human phosphoglucose isomerase and GTP. The biochemical and biological characterization of this binding is described in this chapter. The part II is “Functional analysis of the conserved histidine residue of Bamboo mosaic virus capping enzyme in the activity for the covalent [Enzyme-m7GMP] intermediate formation”. In this part, the amino acid residue that covalently bond to m7GMP was identified using hydroxylamine digestion mapping and mutagenesis assay. The roles of the histidine residue, H66, and the conserved histidine residue, H68, on the formation of [Enzyme-m7GMP] intermediate were also investigated.