A new chemo-enzymatic route to chiral 2-hydroxy-4-phenylbutyrates by combining lactonase-mediated resolution with hydrogenation over Pd/C.

Chem Commun (Camb)

Laboratory of Biocatalysis and Bioprocessing, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai 200237, PR China.

Published: April 2010

A new chemo-enzymatic route to both isomers of 2-hydroxy-4-phenylbutyric acid is reported. The key step is the lactonase-catalyzed hydrolysis of cis- and trans-2-hydroxy-4-phenyl-4-butyrolactones followed by hydrogenation over Pd/C to afford optically pure 2-hydroxy-4-phenylbutyric acid.

Download full-text PDF

Source
http://dx.doi.org/10.1039/b925402aDOI Listing

Publication Analysis

Top Keywords

chemo-enzymatic route
8
hydrogenation pd/c
8
2-hydroxy-4-phenylbutyric acid
8
route chiral
4
chiral 2-hydroxy-4-phenylbutyrates
4
2-hydroxy-4-phenylbutyrates combining
4
combining lactonase-mediated
4
lactonase-mediated resolution
4
resolution hydrogenation
4
pd/c chemo-enzymatic
4

Similar Publications

Benzo[1,4]diazepines show a large diversity of biological activities and are still commonly used as medications against a broad range of diseases. Within our research in the field of chemo-enzymatic alkaloid synthesis, we developed a synthetic route towards close structural relatives, namely benzo[1,4]diazepine-2,5-diones. Possible antimicrobial activities of these substances are barely known up to date.

View Article and Find Full Text PDF

Integrating enzymatic reactions into computer-aided synthesis planning (CASP) should help devise more selective, economical, and greener synthetic routes. Herein we report the triple-transformer loop algorithm with biocatalysis (TTLAB) as a new CASP tool for chemo-enzymatic multistep retrosynthesis. Single-step retrosyntheses are performed using two triple transformer loops (TTL), one trained with chemical reactions from the US Patent Office (USPTO-TTL), the second one obtained by multitask transfer learning combining the USPTO dataset with preparative biotransformations from the literature (ENZR-TTL).

View Article and Find Full Text PDF

Chemo-enzymatic synthesis of NPN cofactor taking advantage of ADP-ribosyl cyclase and LarC cyclometallase promiscuous activities.

Bioorg Chem

December 2024

Department of Chemistry, Laboratory of Bio-Organic Chemistry, Namur Research Institute for Life Sciences (NARILIS), University of Namur (UNamur), 5000 Namur, Belgium. Electronic address:

The nickel-pincer nucleotide cofactor (NPN) is a widespread organometallic cofactor required for lactate racemase (LarA) and for α-hydroxy acid racemases and epimerases of the LarA superfamily. Its biosynthesis, which starts with nicotinic acid adenine dinucleotide (NaAD), requires three enzymes: LarB, LarC, and LarE, and can be performed in vitro with purified enzymes. Nevertheless, as LarE and LarC are single turnover enzymes, the in vitro NPN biosynthesis requires huge amounts of enzymes (particularly 2 equivalents of LarE), which hampers the study of NPN and of NPN-dependent enzymes.

View Article and Find Full Text PDF

Directed Evolution and Immobilization of Lactobacillus brevis Alcohol Dehydrogenase for Chemo-Enzymatic Synthesis of Rivastigmine.

Chemistry

June 2024

National Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, 1 Shizishan Street, Wuhan, 430070, P.R. China.

Rivastigmine is one of the several pharmaceuticals widely prescribed for the treatment of Alzheimer's disease. However, its practical synthesis still faces many issues, such as the involvement of toxic metals and harsh reaction conditions. Herein, we report a chemo-enzymatic synthesis of Rivastigmine.

View Article and Find Full Text PDF

The heterogeneous monomers obtained from plastic waste degradation are unfavorable for PET recondensation and high-value derivative synthesis. Herein, we developed an efficient chemical-enzymatic approach to convert mixed plastic wastes into homogeneous mono-2-hydroxyethyl terephthalate (MHET) without downstream purification, benefiting from three discovered BHETases (KbEst, KbHyd, and BrevEst) in nature. Towards the mixed plastic waste, integrating the chemical KCO-driven glycolysis process with the BHETase depolymerization technique resulted in an MHET yield of up to 98.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!