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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Format: | Final Year Project |
Language: | English |
Published: |
2009
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Subjects: | |
Online Access: | http://hdl.handle.net/10356/15681 |
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Institution: | Nanyang Technological University |
Language: | English |
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. |
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