To access this work you must either be on the Smith College campus OR have valid Smith login credentials.

On Campus users: To access this work if you are on campus please Select the Download button.

Off Campus users: To access this work from off campus, please select the Off-Campus button and enter your Smith username and password when prompted.

Non-Smith users: You may request this item through Interlibrary Loan at your own library.

Publication Date

2019

First Advisor

Cristina Suarez

Document Type

Honors Project

Degree Name

Bachelor of Arts

Department

Chemistry

Keywords

Diels-Alderase, PyrE3, Steroselectivity, QM calculation

Abstract

Catalytic mechanisms for Diels-Alder reaction have been of great interest to researchers even before the discovery of the first natural Diels-Alderase. [1] Many efforts to isolate a standalone natural Diels-Alderase have been successful, and several such Diels-Alderases have been crystallized, but their catalytic mechanisms are not always clear. In 2018, Wen Liu and coworkers [2] crystallized a new natural Diels-Alderase, known as PyrE3, in the biosynthetic pathway for pyrroindomycins. PyrE3 is a mono-functional Diels-Alderase that catalyzes an intramolecular [4+2] cycloaddition, which turns a linear polyene intermediate into a bis-fused cyclic system as shown in Figure 1. During the catalysis, PyrE3 enzyme controls the product stereochemistry and allows the intramolecular Diels-Alder reaction, which has proven inert in the absence of PyrE3.

[FIGURE NOT SHOWN]

Figure 1: PyrE3 catalyzes an intramolecular Diels-Alder reaction in PYR biosynthetic pathway that turns a linear polyene intermediate into a decalin.

In this study, we aim to investigate the catalysis of PyrE3 in two directions: 1) to unravel how PyrE3 reduces the activation barrier to make the reaction happen and enhance the reaction rate; 2) to explain the origin of its stereoselectivity. The main investigative approaches in this study include quantum mechanical calculations, protein-ligand dockings and theozyme calculations.

Rights

©2019 Xingyi Guan. Access limited to the Smith College community and other researchers while on campus. Smith College community members also may access from off-campus using a Smith College log-in. Other off-campus researchers may request a copy through Interlibrary Loan for personal use.

Language

English

Comments

xviii, 95 pages : illustrations (some color). Includes bibliographical references (pages 89-95)

Download

Smith Only:
Off Campus Download

Share

COinS