Enzymatic properties and mutational studies of chalcone synthase from Physcomitrella patens
PpCHS is a member of the type III polyketide synthase family and catalyses the synthesis of the flavonoid precursor naringenin chalcone from p-coumaroyl-CoA. Recent research reports the production of pyrone derivatives using either hexanoyl-CoA or butyryl-CoA as starter molecule. The Cys-His-Asn cat...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI
2012
|
| Online Access: | http://psasir.upm.edu.my/id/eprint/77971/ http://psasir.upm.edu.my/id/eprint/77971/1/77971.pdf |
| _version_ | 1848858377090760704 |
|---|---|
| author | Raja Abdul Rahman, Raja Noor Zaliha Zakaria, Iffah Izzati Salleh, Abu Bakar Basri, Mahiran |
| author_facet | Raja Abdul Rahman, Raja Noor Zaliha Zakaria, Iffah Izzati Salleh, Abu Bakar Basri, Mahiran |
| author_sort | Raja Abdul Rahman, Raja Noor Zaliha |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | PpCHS is a member of the type III polyketide synthase family and catalyses the synthesis of the flavonoid precursor naringenin chalcone from p-coumaroyl-CoA. Recent research reports the production of pyrone derivatives using either hexanoyl-CoA or butyryl-CoA as starter molecule. The Cys-His-Asn catalytic triad found in other plant chalcone synthase predicted polypeptides is conserved in PpCHS. Site directed mutagenesis involving these amino acids residing in the active-site cavity revealed that the cavity volume of the active-site plays a significant role in the selection of starter molecules as well as product formation. Substitutions of Cys 170 with Arg and Ser amino acids decreased the ability of the PpCHS to utilize hexanoyl-CoA as a starter molecule, which directly effected the production of pyrone derivatives (products). These substitutions are believed to have a restricted number of elongations of the growing polypeptide chain due to the smaller cavity volume of the mutant’s active site. |
| first_indexed | 2025-11-15T12:12:28Z |
| format | Article |
| id | upm-77971 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T12:12:28Z |
| publishDate | 2012 |
| publisher | MDPI |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-779712020-05-04T17:55:18Z http://psasir.upm.edu.my/id/eprint/77971/ Enzymatic properties and mutational studies of chalcone synthase from Physcomitrella patens Raja Abdul Rahman, Raja Noor Zaliha Zakaria, Iffah Izzati Salleh, Abu Bakar Basri, Mahiran PpCHS is a member of the type III polyketide synthase family and catalyses the synthesis of the flavonoid precursor naringenin chalcone from p-coumaroyl-CoA. Recent research reports the production of pyrone derivatives using either hexanoyl-CoA or butyryl-CoA as starter molecule. The Cys-His-Asn catalytic triad found in other plant chalcone synthase predicted polypeptides is conserved in PpCHS. Site directed mutagenesis involving these amino acids residing in the active-site cavity revealed that the cavity volume of the active-site plays a significant role in the selection of starter molecules as well as product formation. Substitutions of Cys 170 with Arg and Ser amino acids decreased the ability of the PpCHS to utilize hexanoyl-CoA as a starter molecule, which directly effected the production of pyrone derivatives (products). These substitutions are believed to have a restricted number of elongations of the growing polypeptide chain due to the smaller cavity volume of the mutant’s active site. MDPI 2012 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/77971/1/77971.pdf Raja Abdul Rahman, Raja Noor Zaliha and Zakaria, Iffah Izzati and Salleh, Abu Bakar and Basri, Mahiran (2012) Enzymatic properties and mutational studies of chalcone synthase from Physcomitrella patens. International Journal of Molecular Sciences, 13 (8). pp. 9673-9691. ISSN 1661-6596; ESSN: 1422-0067 https://www.mdpi.com/1422-0067/13/8/9673 10.3390/ijms13089673 |
| spellingShingle | Raja Abdul Rahman, Raja Noor Zaliha Zakaria, Iffah Izzati Salleh, Abu Bakar Basri, Mahiran Enzymatic properties and mutational studies of chalcone synthase from Physcomitrella patens |
| title | Enzymatic properties and mutational studies of chalcone synthase from Physcomitrella patens |
| title_full | Enzymatic properties and mutational studies of chalcone synthase from Physcomitrella patens |
| title_fullStr | Enzymatic properties and mutational studies of chalcone synthase from Physcomitrella patens |
| title_full_unstemmed | Enzymatic properties and mutational studies of chalcone synthase from Physcomitrella patens |
| title_short | Enzymatic properties and mutational studies of chalcone synthase from Physcomitrella patens |
| title_sort | enzymatic properties and mutational studies of chalcone synthase from physcomitrella patens |
| url | http://psasir.upm.edu.my/id/eprint/77971/ http://psasir.upm.edu.my/id/eprint/77971/ http://psasir.upm.edu.my/id/eprint/77971/ http://psasir.upm.edu.my/id/eprint/77971/1/77971.pdf |