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The Molecular Design, Soluble Expression and Characterization of a Thermostable Chimeric Esterase

Author: ZhangYuHang
Tutor: FengYan
School: Jilin University
Course: Microbial and Biochemical Pharmacy
Keywords: α / β hydrolase superfamily Chimeric enzymes Rational Design Substrate selectivity Soluble expression
CLC: R914
Type: Master's thesis
Year: 2007
Downloads: 129
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Abstract


Derived from the thermophilic acyl the aminopeptidase ( APE1547 ) in Archaea Aeropyrum pernix K1 derived from the ancient bacteria Archaeoglobus fulgidus the thermophilic esterase ( AFEST ) having a structure similar to the α / β hydrolase fold domain (RMSD 2.6 ) , both but there are obvious differences in the catalytic properties and substrate specificity . In this paper, molecular design as a means , domain restructuring , the study the structure area outside the α / β hydrolase superfamily in the α / β hydrolase domain selectivity and stability of the enzyme substrate . In this paper, the LPC / CSU server ( Ligand - Protein the Contacts the Contacts of Structural Units ) Analysis of the the the natural AFEST APE1547 structures α / β hydrolase domain of the connection area between other structural domain structure characteristics , select the mode of action between the two parental most similar loci as a recombination site , structure of AFEST the cap with APE1547 R526V mutants of the α / β hydrolase fold domain fusion ; homology modeling program Modeller established a molecular model of the chimeric enzyme by PROCHECK the software such model assessment ; mutation most likely to affect the recombinant protein soluble residues ; After optimization of culture and purification conditions , and ultimately to obtain a soluble chimeric enzymes AAM6 of ; results show AAM6 retained thermal stability of the parents characteristics ; compared with APE1547 , , loss of peptidase activity , esterase activity and the presence can be detected , and the short chain substrate specificity biased substrate . Molecular dynamics simulations (Molecular Dynamic) for this experimental phenomenon . In this paper, the rational design methods , recombination between the α / β hydrolase superfamily nonhomologous protein α / β structure outside its structural components for further study of the α / β hydrolase superfamily \the influence of the substrate specificity provide an experimental basis .

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