Cover Image

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

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...

Full description

Saved in:
Bibliographic Details
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
http://eprints.usm.my/42219/
Tags: Add Tag
No Tags, Be the first to tag this record!
id my.usm.eprints.42219
record_format eprints
spelling my.usm.eprints.42219 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.
institution Universiti Sains Malaysia
building Hamzah Sendut Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Sains Malaysia
content_source USM Institutional Repository
url_provider http://eprints.usm.my/
language English
topic QH1 Natural history (General - Including nature conservation, geographical distribution)
spellingShingle QH1 Natural history (General - Including nature conservation, geographical distribution)
Arsad, Hasni
Determination Of R-3-Hydroxyacylacp- Coa Transferase (Phag) Structure
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.
format Thesis
author Arsad, Hasni
author_facet Arsad, Hasni
author_sort Arsad, Hasni
title Determination Of R-3-Hydroxyacylacp- Coa Transferase (Phag) Structure
title_short 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_sort determination of r-3-hydroxyacylacp- coa transferase (phag) structure
publishDate 2010
url http://eprints.usm.my/42219/1/Hasni_Bin_Arsad24.pdf
http://eprints.usm.my/42219/
_version_ 1643710443146969088
score 13.211869

Similar Items