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

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

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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 potentia...

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Main Author: Arsad, Hasni
Format: Thesis
Language:English
Published: 2010
Subjects:
QH1 Natural history (General - Including nature conservation, geographical distribution)
Online Access:http://eprints.usm.my/42219/1/Hasni_Bin_Arsad24.pdf
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author Arsad, Hasni
author_facet Arsad, Hasni
author_sort Arsad, Hasni
collection USM
description 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.
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spelling usm.eprints-422192019-04-12T05:26:55Z http://eprints.usm.my/42219/ Determination Of R-3-Hydroxyacylacp- Coa Transferase (Phag) Structure Arsad, Hasni QH1 Natural history (General - Including nature conservation, geographical distribution) 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. 2010-03 Thesis NonPeerReviewed application/pdf en http://eprints.usm.my/42219/1/Hasni_Bin_Arsad24.pdf Arsad, Hasni (2010) Determination Of R-3-Hydroxyacylacp- Coa Transferase (Phag) Structure. PhD thesis, Universiti Sains Malaysia.
spellingShingle QH1 Natural history (General - Including nature conservation, geographical distribution)
Arsad, Hasni
Determination Of R-3-Hydroxyacylacp- Coa Transferase (Phag) Structure
title Determination Of R-3-Hydroxyacylacp- Coa Transferase (Phag) Structure
title_full Determination Of R-3-Hydroxyacylacp- Coa Transferase (Phag) Structure
title_fullStr Determination Of R-3-Hydroxyacylacp- Coa Transferase (Phag) Structure
title_full_unstemmed Determination Of R-3-Hydroxyacylacp- Coa Transferase (Phag) Structure
title_short Determination Of R-3-Hydroxyacylacp- Coa Transferase (Phag) Structure
title_sort determination of r 3 hydroxyacylacp coa transferase phag structure
topic QH1 Natural history (General - Including nature conservation, geographical distribution)
url http://eprints.usm.my/42219/1/Hasni_Bin_Arsad24.pdf
work_keys_str_mv AT arsadhasni determinationofr3hydroxyacylacpcoatransferasephagstructure

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