Determination Of R-3-Hydroxyacylacp- Coa Transferase (Phag) Structure

Arsad, Hasni (2010) Determination Of R-3-Hydroxyacylacp- Coa Transferase (Phag) Structure. ["eprint_fieldopt_thesis_type_phd" not defined] thesis, Universiti Sains Malaysia.

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Abstract

R-3-hydroxyacyl-ACP-CoA transferase (PhaG) catalyzes the conversion of (R)-3- hydroxyacyl-ACP to (R)-3-hydroxyacyl-CoA derivatives, which serve as the ultimate precursor for polyhydroxyalkanoate (PHA) polymerization from unrelated substrates. PHA is a family of bioplastic that has a good potential to replace fossilbased thermoplastics because it is biodegradable. The transferase enzyme PhaG of a locally isolated strain, Pseudomonas sp. USM 4-55, was recently cloned (GeneBank accession number EU305558). Currently there is no known 3D structure with high similarity to PhaG. In order to over express, the phaG gene was cloned into expression vector pQE-30 and it was successfully overexpressed by induction with 0.5 mM IPTG in the host Escherichia coli strain SG 13009.

Item Type: Thesis (["eprint_fieldopt_thesis_type_phd" not defined])
Subjects: Q Science > QH Natural history > QH1 Natural history (General - Including nature conservation, geographical distribution)
Divisions: Pusat Pengajian Sains Kajihayat (School of Biological Sciences) > Thesis
Depositing User: Mr Mohammad Harish Sabri
Date Deposited: 01 Oct 2018 01:39
Last Modified: 01 Oct 2018 01:39
URI: http://eprints.usm.my/id/eprint/42219

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