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...
محفوظ في:
| المؤلف الرئيسي: | |
|---|---|
| التنسيق: | أطروحة |
| اللغة: | English |
| منشور في: |
2010
|
| الموضوعات: | |
| الوصول للمادة أونلاين: | http://eprints.usm.my/42219/1/Hasni_Bin_Arsad24.pdf |
| الوسوم: |
إضافة وسم
لا توجد وسوم, كن أول من يضع وسما على هذه التسجيلة!
|
| id |
my-usm-ep.42219 |
|---|---|
| record_format |
uketd_dc |
| spelling |
my-usm-ep.422192019-04-12T05:26:55Z Determination Of R-3-Hydroxyacylacp- Coa Transferase (Phag) Structure 2010-03 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 http://eprints.usm.my/42219/ http://eprints.usm.my/42219/1/Hasni_Bin_Arsad24.pdf application/pdf en public phd doctoral Universiti Sains Malaysia Pusat Pengajian Sains Kajihayat |
| institution |
Universiti Sains Malaysia |
| collection |
USM Institutional Repository |
| 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 |
| qualification_name |
Doctor of Philosophy (PhD.) |
| qualification_level |
Doctorate |
| 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 |
| granting_institution |
Universiti Sains Malaysia |
| granting_department |
Pusat Pengajian Sains Kajihayat |
| publishDate |
2010 |
| url |
http://eprints.usm.my/42219/1/Hasni_Bin_Arsad24.pdf |
| _version_ |
1747821036655607808 |