An industrially applied biocatalyst: 2-Deoxy-d-ribose-5- phosphate aldolase. (December 2017)

• Record Type: Journal Article
• Authors: Fei, Hui; Zheng, Cheng-cai; Liu, Xin-ye; Li, Qian
• Is Part Of: Process biochemistry. Volume 63(2017)
• Page Start: 55
• Page End: 59
• Publication Date: 2017-12
• Subjects: 2-Deoxy-d-ribose-5-phosphate aldolase -- Aldehyde tolerance -- Catalytic activity -- Protein engineering -- Computational design -- Immobilization; Biochemical engineering -- Periodicals; Biotechnology -- Periodicals; Biochemistry -- periodicals; Biotechnology -- periodicals; Chemical Engineering -- periodicals; Génie biochimique -- Périodiques; Biotechnologie -- Périodiques; Biochemical engineering; Biotechnology; Periodicals; 660.63
• DOI: 10.1016/j.procbio.2017.08.001
• Languages: English
• ISSNs: 1359-5113

Abstract

Highlights: 2-Deoxy-d -ribose-5-phosphate aldolase(DERA) can form C–C bonds to generate multiple chiral centers, which provides an interesting route for the production of key chiral compounds. However, several problems such as low activity and poor stability (poor tolerance to high concentration of aldehyde) limit the practical application of DERA for large-scale production. Many new DERAs have been cloned from various extreme microorganisms, with high catalytic activity or excellent aldehyde tolerance. Based on analysis of the catalytic mechanism of DERA, rational design engineering and computational design have been used to reconstruct enzymes to alter the stability and catalytic activity of DERA. Abstract: 2-Deoxy-d -ribose-5-phosphate aldolase (DERA) belongs to the family of lyases and can form C–C bonds to generate multiple chiral centers, thus providing an interesting route to produce key chiral compounds. However, several problems, such as low activity and poor stability (poor tolerance to high aldehyde concentrations), limit the practical application of DERA in large-scale production. Many approaches have been introduced to address these issues. Specifically, in the last decade, many new DERAs, with high catalytic activity or excellent aldehyde tolerance, have been cloned from various extremophilic microorganisms. In addition, on the basis of the analysis of the catalytic mechanism of DERA, rational design engineering and computational design have been used to reconstruct DERA enzymes to alter their stability and catalytic activity.