溶藻弧菌胺醯組胺酸雙胜肽酶之晶體結構與突變分析

張晉源

doi:10.6842/NCTU.2011.00702

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溶藻弧菌胺醯組胺酸雙胜肽酶之晶體結構與突變分析

Crystal Structure and Mutational Analysis of Aminoacylhistidine Dipeptidase (PepD) from Vibrio alginolyticus

張晉源 , Ph.D　　Advisor：吳東昆　　

英文 DOI： 10.6842/NCTU.2011.00702

溶藻弧菌；胺醯組胺酸雙胜肽酶；晶體結構；突變分析；肌雙胜；兒茶酚；水解酶；氧化酶； Vibrio alginolyticus ； Aminoacylhistidine dipeptidase ； Crystal structure ； Mutational analysis ； Carnosine ； Catechol ； Hydrolase ； Oxidase

Abstract │ Reference (91) │ Altmetrics

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Aminoacylhistidine dipeptidase (PepD, EC 3.4.13.3), a member of peptidase M20 family, exhibits a broad substrate specificity for unusual dipeptides carnosine (β-Ala-L-His) and homocarnosine (γ-aminobutyl-His) and a few tripeptides. Basically, PepD catalyzes the cleavage and release of N-terminal amino acid from Xaa-His dipeptide molecules. In this thesis, the PepD from Vibrio alginolyticus was physically and chemically characterized for protein 3D structure, biochemical property, and metal-catalyzed mechanism. The 3D structure was solved by X-ray crystallography, showing that PepD is a homodimer. Each monomeric subunit of the homodimer is composed of a lid domain and a catalytic domain, in which two zinc ions dwell in the active site. In distinction to other M20 family enzymes, the PepD’s dimeric structure exhibits a unique criss-cross configuration that is likely formed through interface interaction of respective lid domains. By performing mutational analysis, crucial residues were identified for maintaining PepD architecture, substrate recognition and enzymatic activity. In addition, changing the active site zinc ions with copper ions, converts PepD to catechol oxidase. The CuCu-PepD is able to oxidize catechol derivatives with a polar tail, but not catechol or 3,5-di-tert-butylcatechol (DTC) that carries non-polar side chains. This result agrees with protein-ligand docking analysis. Collectively, this study advances our overall understanding for aminoacylhistidine dipeptidase in the structure-activity relationships and facilitates future development of antibody-directed enzyme prodrug therapy (ADEPT). Most importantly, the identification of PepD functionality conversion from peptidase to oxidase has paved a new avenue for divergent enzyme evolution.

Reference ( 91 ) 〈TOP〉

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