Cargando…
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...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Molecular Diversity Preservation International (MDPI)
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3431822/ https://www.ncbi.nlm.nih.gov/pubmed/22949824 http://dx.doi.org/10.3390/ijms13089673 |
_version_ | 1782242109135257600 |
---|---|
author | Rahman, Raja Noor Zaliha Raja Abdul Zakaria, Iffah Izzati Salleh, Abu Bakar Basri, Mahiran |
author_facet | Rahman, Raja Noor Zaliha Raja Abdul Zakaria, Iffah Izzati Salleh, Abu Bakar Basri, Mahiran |
author_sort | Rahman, Raja Noor Zaliha Raja Abdul |
collection | PubMed |
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. |
format | Online Article Text |
id | pubmed-3431822 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Molecular Diversity Preservation International (MDPI) |
record_format | MEDLINE/PubMed |
spelling | pubmed-34318222012-09-04 Enzymatic Properties and Mutational Studies of Chalcone Synthase from Physcomitrella patens Rahman, Raja Noor Zaliha Raja Abdul Zakaria, Iffah Izzati Salleh, Abu Bakar Basri, Mahiran Int J Mol Sci Article 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. Molecular Diversity Preservation International (MDPI) 2012-08-03 /pmc/articles/PMC3431822/ /pubmed/22949824 http://dx.doi.org/10.3390/ijms13089673 Text en © 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Rahman, Raja Noor Zaliha Raja Abdul 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 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3431822/ https://www.ncbi.nlm.nih.gov/pubmed/22949824 http://dx.doi.org/10.3390/ijms13089673 |
work_keys_str_mv | AT rahmanrajanoorzaliharajaabdul enzymaticpropertiesandmutationalstudiesofchalconesynthasefromphyscomitrellapatens AT zakariaiffahizzati enzymaticpropertiesandmutationalstudiesofchalconesynthasefromphyscomitrellapatens AT sallehabubakar enzymaticpropertiesandmutationalstudiesofchalconesynthasefromphyscomitrellapatens AT basrimahiran enzymaticpropertiesandmutationalstudiesofchalconesynthasefromphyscomitrellapatens |