Literature DB >> 19760118

Diastereoselective synthesis of L: -threo-3,4-dihydroxyphenylserine by low-specific L: -threonine aldolase mutants.

Hui-Jeong Gwon1, Sang-Ho Baik.   

Abstract

Diastereoselectivity-enhanced mutants of L: -threonine aldolase (L: -TA) for L: -threo-3,4-dihydroxyphenylserine (L: -threo-DOPS) synthesis were isolated by error-prone PCR followed by a high-throughput screening. The most improved mutant was achieved from the mutant T3-3mm2, showing a 4-fold increase over the wild-type L: -TA. When aldol condensation activity was examined using whole cells of T3-3mm2, its de was constantly maintained at 55% during the batch reactions for 80 h, yielding 3.8 mg L: -threo-DOPS/ml.

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Year:  2009        PMID: 19760118     DOI: 10.1007/s10529-009-0125-z

Source DB:  PubMed          Journal:  Biotechnol Lett        ISSN: 0141-5492            Impact factor:   2.461


  3 in total

1.  On the catalytic mechanism and stereospecificity of Escherichia coli L-threonine aldolase.

Authors:  Martino L di Salvo; Soumya G Remesh; Mirella Vivoli; Mohini S Ghatge; Alessandro Paiardini; Simona D'Aguanno; Martin K Safo; Roberto Contestabile
Journal:  FEBS J       Date:  2013-11-13       Impact factor: 5.542

Review 2.  Threonine aldolases: perspectives in engineering and screening the enzymes with enhanced substrate and stereo specificities.

Authors:  Kateryna Fesko
Journal:  Appl Microbiol Biotechnol       Date:  2016-01-26       Impact factor: 4.813

3.  Application of Threonine Aldolases for the Asymmetric Synthesis of α-Quaternary α-Amino Acids.

Authors:  Julia Blesl; Melanie Trobe; Felix Anderl; Rolf Breinbauer; Gernot A Strohmeier; Kateryna Fesko
Journal:  ChemCatChem       Date:  2018-07-04       Impact factor: 5.686

  3 in total

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