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| http://dx.doi.org/10.1002/ange.201209946 | DOI Listing |
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Active Site Engineering of a Glycerol Dehydrogenase Improves its Oxidative Activity and Scope Toward Glycerol Derivatives.
Chemistry
January 2025
Heterogeneous Biocatalysis Laboratory, CICbiomaGUNE, Basque Research and Technology Alliance (BRTA), Paseo Miramón, 194, Donostia-San Sebastián, 20014, Spain.
Regioselective oxidation of glyceryl alkyl ethers is of utmost importance for the fabrication of substituted hydroxy ketones and enantiopure 1,2-diols as green solvents and pharmaceutical building blocks, respectively. An engineered glycerol dehydrogenase from Bacillus stearothermophilus was described to perform the regioselective oxidation of alkyl glycerol ethers, identifying position 252 as key for accepting larger substrates than glycerol. In this work, we further engineer that position through partial saturation mutagenesis to broaden the substrate scope toward other glycerol derivatives, improving enzyme kinetics and minimizing product inhibition.
View Article and Find Full Text PDFOne-Pot Two-Stage Biocatalytic Cascade to Produce l-Phosphinothricin by Two Enantioselective Complementary Aminotransferases at High Substrate Loading via a Deracemization Process.
J Agric Food Chem
June 2024
State Key Laboratory of Bioreactor Engineering East China University of Science and Technology, Shanghai 200237, China.
The bioderacemization of racemic phosphinothricin (D, L-PPT) is a promising route for the synthesis of l-phosphinothricin (L-PPT). However, the low activity and tolerance of wild-type enzymes restrict their industrial applications. Two stereocomplementary aminotransferases with high activity and substrate tolerance were identified in a metagenomic library, and a one-pot, two-stage artificial cascade biocatalytic system was developed to produce L-PPT through kinetic resolution and asymmetric amination.
View Article and Find Full Text PDFBifunctional Chiral Agent Enables One-pot Spontaneous Deracemization of Racemic Compounds.
Angew Chem Int Ed Engl
May 2024
School of Chemical Engineering and Technology, State Key Laboratory of Chemical Engineering, Tianjin University; The Co-Innovation Centre of Chemistry and Chemical Engineering of Tianjin, Tianjin, 300072, P. R. China.
A novel one-pot deracemization method using a bifunctional chiral agent (BCA) is proposed for the first time to convert a racemate to the desired enantiomer. Specifically, chiral α, (α-diphenyl-2-pyrrolidinemethanol) formed enantiospecific cocrystals with racemic dihydromyricetin, and used its own alkaline catalysis to catalyze the racemization between the (2R,3R)-enantiomer and (2S,3S)-enantiomer in solution, achieving a one-pot spontaneous deracemization. This strategy was also successfully extended to the deracemization of three other racemic compound drugs: (R,S)-carprofen, (R,S)-indoprofen, and (R,S)-indobufen.
View Article and Find Full Text PDFDevelopment of an Enzyme Cascade System for the Synthesis of Enantiomerically Pure D-Amino Acids Utilizing Ancestral L-Amino Acid Oxidase.
Chembiochem
April 2024
Graduate Division of Nutritional and Environmental Sciences, University of Shizuoka 52-1 Yada, Suruga-ku, Shizuoka, 422-8526, Japan for S.N.
Article Synopsis
- Enantiomerically pure D-amino acids can be used to create various fine chemicals, especially in the pharmaceutical industry, making them highly valuable.
- This study presents a new enzymatic cascade that converts L-amino acids into D-amino acids by using four specific enzymes to facilitate different steps in the process.
- After optimizing conditions, the system successfully produced five different D-amino acids, showing high enantiopurity, indicating its effectiveness for producing a range of D-amino acids.
Identification of a novel thermostable transaminase and its application in L-phosphinothricin biosynthesis.
Appl Microbiol Biotechnol
January 2024
Joint Engineering Research Center for Biomanufacturing of Chiral Chemicals, The National and Local, Zhejiang University of Technology, Hangzhou, 310014, People's Republic of China.
Transaminase (TA) is a crucial biocatalyst for enantioselective production of the herbicide L-phosphinothricin (L-PPT). The use of enzymatic cascades has been shown to effectively overcome the unfavorable thermodynamic equilibrium of TA-catalyzed transamination reaction, also increasing demand for TA stability. In this work, a novel thermostable transaminase (PtTA) from Pseudomonas thermotolerans was mined and characterized.
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