Consulta: creatorFacets:"Yunmian He"
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Data/hora: 11/06/2024 01:27:50

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