Consulta: creatorFacets:"Yijun Chen"
Registros recuperados: 4
Data/hora: 16/06/2024 04:10:50

A Bacterial Enzyme Catalyzing Double Reduction of a &amp;#x3b2;,&amp;#x3b4;-Diketo Ester with Unprecedented Stereoselectivity
Provedor de dados: 17
Autores: Xuri Wu; Nan Liu; Yunmian He; Yijun Chen.
Various ketoreductases exclusively participate in all common biological events, and they are a class of important biocatalysts for the production of chiral alcohols. While many types of ketoreductase have been extensively studied and their functions, properties and utilities have been well known, the capability of stereoselectively reducing two carbonyl groups in the same diketohexanoate ester molecule to form a dihydroxy product by a single ketoreductase has not been evidently characterized. Here we show that a unique and novel enzyme, diketoreductase, was cloned from Acinetobacter baylyi, heterogeneously expressed in _Escherichia coli_ and purified to homogeneity. The diketoreductase is up to 78% homologous to bacterial 3-hydroxyacyl coenzyme-A...
Tipo: Manuscript
Palavras-chave: Biotechnology; Chemistry; Microbiology.
Ano: 2008
URL: http://precedings.nature.com/documents/1697/version/1

A Bacterial Enzyme Catalyzing Double Reduction of a &amp;#x3b2;,&amp;#x3b4;-Diketo Ester with Unprecedented Stereoselectivity
Provedor de dados: 17
Autores: Xuri Wu; Nan Liu; Yunmian He; Yijun Chen.
Various ketoreductases exclusively participate in all common biological events, and they are a class of important biocatalysts for the production of chiral alcohols. While many types of ketoreductase have been extensively studied and their functions, properties and utilities have been well known, the capability of stereoselectively reducing two carbonyl groups in the same diketohexanoate ester molecule to form a dihydroxy product by a single ketoreductase has not been evidently characterized. Here we show that a unique and novel enzyme, diketoreductase, was cloned from Acinetobacter baylyi, heterogeneously expressed in _Escherichia coli_ and purified to homogeneity. The diketoreductase is up to 78% homologous to bacterial 3-hydroxyacyl coenzyme-A...
Tipo: Manuscript
Palavras-chave: Biotechnology; Chemistry; Microbiology.
Ano: 2010
URL: http://precedings.nature.com/documents/1697/version/2

Simple reverse genetics approach to elucidating the biosynthetic pathway of complex thiopeptide nocathiacin
Provedor de dados: 17
Autores: Maochen Wei; Jing Deng; Shuzhen Wang; Nan Liu; Yijun Chen.
Biothythetic pathway of the most drugable thiopeptide nocathiacin has been elucidated by applying reverse genetics method based on its structural features. The present study provides an efficient approach for an easy access to the biosynthetic gene clusters of complex bioactive peptides that are ribosomally synthesized with extensive posttranslational modifications.
Tipo: Manuscript
Palavras-chave: Biotechnology; Genetics &amp; Genomics; Microbiology; Bioinformatics.
Ano: 2010
URL: http://precedings.nature.com/documents/4740/version/1

Genetic incorporation of D-Lysine into diketoreductase in Escherichia coli cells
Provedor de dados: 17
Autores: Zhi Zhi Liu; Xin Yang; Denghuan Yi; Shuzhen Wang; Yijun Chen.
D-Lysine has been genetically introduced into diketoreductase in E. coli cells by utilization of an orthogonal Ph tRNA /Lysyl-tRNA synthetase pair. This is the first report on the genetic incoporation of D-amino acids into proteins, which may be generally applicable to a wide variety of applications.
Tipo: Manuscript
Palavras-chave: Biotechnology; Chemistry; Microbiology; Molecular Cell Biology.
Ano: 2012
URL: http://precedings.nature.com/documents/6777/version/1