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Enzymatic synthesis of 2-hydroxy-4H-quinolizin-4-one scaffolds by integrating coenzyme a ligases and a type III PKS from Huperzia serrata
2-Hydroxy-4H-quinolizin-4-one scaffolds were enzymatically synthesized by integrating three enzymes including phenylacetate-CoA ligase (PcPCL) from an endophytic fungus Penicillium chrysogenum MT-12, malonyl-CoA synthase (AtMatB) from Arabidopsis thaliana, and a type III polyketide synthase (HsPKS3)...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9054772/ https://www.ncbi.nlm.nih.gov/pubmed/35517366 http://dx.doi.org/10.1039/d0ra04133e |
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author | Wang, Juan Ding, Ning Wu, Yun Shi, Xiaoping Qi, Bowen Liu, Xiao Wang, Xiaohui Li, Jun Tu, Pengfei Shi, Shepo |
author_facet | Wang, Juan Ding, Ning Wu, Yun Shi, Xiaoping Qi, Bowen Liu, Xiao Wang, Xiaohui Li, Jun Tu, Pengfei Shi, Shepo |
author_sort | Wang, Juan |
collection | PubMed |
description | 2-Hydroxy-4H-quinolizin-4-one scaffolds were enzymatically synthesized by integrating three enzymes including phenylacetate-CoA ligase (PcPCL) from an endophytic fungus Penicillium chrysogenum MT-12, malonyl-CoA synthase (AtMatB) from Arabidopsis thaliana, and a type III polyketide synthase (HsPKS3) from Chinese club moss Huperzia serrata. The findings paved the way to produce these kinds of structurally interesting alkaloids by engineered microorganisms. |
format | Online Article Text |
id | pubmed-9054772 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | The Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-90547722022-05-04 Enzymatic synthesis of 2-hydroxy-4H-quinolizin-4-one scaffolds by integrating coenzyme a ligases and a type III PKS from Huperzia serrata Wang, Juan Ding, Ning Wu, Yun Shi, Xiaoping Qi, Bowen Liu, Xiao Wang, Xiaohui Li, Jun Tu, Pengfei Shi, Shepo RSC Adv Chemistry 2-Hydroxy-4H-quinolizin-4-one scaffolds were enzymatically synthesized by integrating three enzymes including phenylacetate-CoA ligase (PcPCL) from an endophytic fungus Penicillium chrysogenum MT-12, malonyl-CoA synthase (AtMatB) from Arabidopsis thaliana, and a type III polyketide synthase (HsPKS3) from Chinese club moss Huperzia serrata. The findings paved the way to produce these kinds of structurally interesting alkaloids by engineered microorganisms. The Royal Society of Chemistry 2020-06-22 /pmc/articles/PMC9054772/ /pubmed/35517366 http://dx.doi.org/10.1039/d0ra04133e Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/ |
spellingShingle | Chemistry Wang, Juan Ding, Ning Wu, Yun Shi, Xiaoping Qi, Bowen Liu, Xiao Wang, Xiaohui Li, Jun Tu, Pengfei Shi, Shepo Enzymatic synthesis of 2-hydroxy-4H-quinolizin-4-one scaffolds by integrating coenzyme a ligases and a type III PKS from Huperzia serrata |
title | Enzymatic synthesis of 2-hydroxy-4H-quinolizin-4-one scaffolds by integrating coenzyme a ligases and a type III PKS from Huperzia serrata |
title_full | Enzymatic synthesis of 2-hydroxy-4H-quinolizin-4-one scaffolds by integrating coenzyme a ligases and a type III PKS from Huperzia serrata |
title_fullStr | Enzymatic synthesis of 2-hydroxy-4H-quinolizin-4-one scaffolds by integrating coenzyme a ligases and a type III PKS from Huperzia serrata |
title_full_unstemmed | Enzymatic synthesis of 2-hydroxy-4H-quinolizin-4-one scaffolds by integrating coenzyme a ligases and a type III PKS from Huperzia serrata |
title_short | Enzymatic synthesis of 2-hydroxy-4H-quinolizin-4-one scaffolds by integrating coenzyme a ligases and a type III PKS from Huperzia serrata |
title_sort | enzymatic synthesis of 2-hydroxy-4h-quinolizin-4-one scaffolds by integrating coenzyme a ligases and a type iii pks from huperzia serrata |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9054772/ https://www.ncbi.nlm.nih.gov/pubmed/35517366 http://dx.doi.org/10.1039/d0ra04133e |
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