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...
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| Format: | Thesis |
| Language: | English |
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2010
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| Online Access: | http://eprints.usm.my/42219/ http://eprints.usm.my/42219/1/Hasni_Bin_Arsad24.pdf |
| _version_ | 1848879500948930560 |
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| author | Arsad, Hasni |
| author_facet | Arsad, Hasni |
| author_sort | Arsad, Hasni |
| building | USM Institutional Repository |
| collection | Online Access |
| 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. |
| first_indexed | 2025-11-15T17:48:14Z |
| format | Thesis |
| id | usm-42219 |
| institution | Universiti Sains Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T17:48:14Z |
| publishDate | 2010 |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | usm-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/ http://eprints.usm.my/42219/1/Hasni_Bin_Arsad24.pdf |