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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...

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Autores principales: Rahman, Raja Noor Zaliha Raja Abdul, Zakaria, Iffah Izzati, Salleh, Abu Bakar, Basri, Mahiran
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
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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.
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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
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