Protease-catalysed Direct Asymmetric Mannich Reaction in Organic Solvent

We reported the first enzyme-catalysed, direct, three-component asymmetric Mannich reaction using protease type XIV from Streptomyces griseus (SGP) in acetonitrile. Yields of up to 92% with enantioselectivities of up to 88% e.e. and diastereoselectivities of up to 92:8 (syn:anti) were achieved under...

Descripción completa

Detalles Bibliográficos
Autores principales: Xue, Yang, Li, Ling-Po, He, Yan-Hong, Guan, Zhi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2012
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3478581/
https://www.ncbi.nlm.nih.gov/pubmed/23094136
http://dx.doi.org/10.1038/srep00761
_version_ 1782247333638963200
author Xue, Yang
Li, Ling-Po
He, Yan-Hong
Guan, Zhi
author_facet Xue, Yang
Li, Ling-Po
He, Yan-Hong
Guan, Zhi
author_sort Xue, Yang
collection PubMed
description We reported the first enzyme-catalysed, direct, three-component asymmetric Mannich reaction using protease type XIV from Streptomyces griseus (SGP) in acetonitrile. Yields of up to 92% with enantioselectivities of up to 88% e.e. and diastereoselectivities of up to 92:8 (syn:anti) were achieved under the optimised conditions. This enzyme's catalytic promiscuity expands the application of this biocatalyst and provides a potential alternative method for asymmetric Mannich reactions.
format Online
Article
Text
id pubmed-3478581
institution National Center for Biotechnology Information
language English
publishDate 2012
publisher Nature Publishing Group
record_format MEDLINE/PubMed
spelling pubmed-34785812012-10-23 Protease-catalysed Direct Asymmetric Mannich Reaction in Organic Solvent Xue, Yang Li, Ling-Po He, Yan-Hong Guan, Zhi Sci Rep Article We reported the first enzyme-catalysed, direct, three-component asymmetric Mannich reaction using protease type XIV from Streptomyces griseus (SGP) in acetonitrile. Yields of up to 92% with enantioselectivities of up to 88% e.e. and diastereoselectivities of up to 92:8 (syn:anti) were achieved under the optimised conditions. This enzyme's catalytic promiscuity expands the application of this biocatalyst and provides a potential alternative method for asymmetric Mannich reactions. Nature Publishing Group 2012-10-23 /pmc/articles/PMC3478581/ /pubmed/23094136 http://dx.doi.org/10.1038/srep00761 Text en Copyright © 2012, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by/3.0/ This work is licensed under a Creative Commons Attribution 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by/3.0/
spellingShingle Article
Xue, Yang
Li, Ling-Po
He, Yan-Hong
Guan, Zhi
Protease-catalysed Direct Asymmetric Mannich Reaction in Organic Solvent
title Protease-catalysed Direct Asymmetric Mannich Reaction in Organic Solvent
title_full Protease-catalysed Direct Asymmetric Mannich Reaction in Organic Solvent
title_fullStr Protease-catalysed Direct Asymmetric Mannich Reaction in Organic Solvent
title_full_unstemmed Protease-catalysed Direct Asymmetric Mannich Reaction in Organic Solvent
title_short Protease-catalysed Direct Asymmetric Mannich Reaction in Organic Solvent
title_sort protease-catalysed direct asymmetric mannich reaction in organic solvent
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3478581/
https://www.ncbi.nlm.nih.gov/pubmed/23094136
http://dx.doi.org/10.1038/srep00761
work_keys_str_mv AT xueyang proteasecatalyseddirectasymmetricmannichreactioninorganicsolvent
AT lilingpo proteasecatalyseddirectasymmetricmannichreactioninorganicsolvent
AT heyanhong proteasecatalyseddirectasymmetricmannichreactioninorganicsolvent
AT guanzhi proteasecatalyseddirectasymmetricmannichreactioninorganicsolvent

Ejemplares similares