Site directed mutagenesis of alkyl hydroperoxide reductase.

This research was designed to investigate the binding site of nicotinamide adenine dinucleotide (NADH) on alkyl hydroperoxide reductase subunit F (AhpF) of Salmonella typhimurium by using site directed mutagenesis. The postulated binding site was suggested by using molecular mechanics Poisson–Bol...

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Bibliographic Details
Main Author: Tee, Chiu Seng.
Other Authors: Jiang Rongrong
Format: Final Year Project
Language:English
Published: 2009
Subjects:
Online Access:http://hdl.handle.net/10356/15681
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Institution: Nanyang Technological University
Language: English
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Summary:This research was designed to investigate the binding site of nicotinamide adenine dinucleotide (NADH) on alkyl hydroperoxide reductase subunit F (AhpF) of Salmonella typhimurium by using site directed mutagenesis. The postulated binding site was suggested by using molecular mechanics Poisson–Boltzmann surface area (MM/PBSA) approach. AhpF enzyme requires NADH as a cofactor to function properly in peroxide reductase catalysis. The wild type AhpF was mutated in such a way that it could no longer bind to NADH as postulated by MM/PBSA approach. The hypothetical binding site would be proven correct if the activity of the mutant enzyme decreases significantly from the wild type.