Literature DB >> 14507195

An efficient and selective enzymatic oxidation system for the synthesis of enantiomerically pure D-tert-leucine.

Werner Hummel1, Mutlu Kuzu, Birgit Geueke.   

Abstract

[reaction: see text] d-tert-Leucine was prepared with an enantiomeric excess of >99% by an enzyme-catalyzed oxidative resolution of the racemic mixture of dl-tert-leucine with use of leucine dehydrogenase. The l-amino acid was oxidized completely due to coupling of the primary reaction with a highly efficient irreversible NAD(+)-regenerating step by NADH oxidase.

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Year:  2003        PMID: 14507195     DOI: 10.1021/ol035314g

Source DB:  PubMed          Journal:  Org Lett        ISSN: 1523-7052            Impact factor:   6.005


  3 in total

1.  Active-Site Engineering of ω-Transaminase for Production of Unnatural Amino Acids Carrying a Side Chain Bulkier than an Ethyl Substituent.

Authors:  Sang-Woo Han; Eul-Soo Park; Joo-Young Dong; Jong-Shik Shin
Journal:  Appl Environ Microbiol       Date:  2015-07-31       Impact factor: 4.792

2.  Enantioselective, ketoreductase-based entry into pharmaceutical building blocks: ethanol as tunable nicotinamide reductant.

Authors:  Sylvain Broussy; Ross W Cheloha; David B Berkowitz
Journal:  Org Lett       Date:  2009-01-15       Impact factor: 6.005

3.  Cofactor Specificity Engineering of Streptococcus mutans NADH Oxidase 2 for NAD(P)(+) Regeneration in Biocatalytic Oxidations.

Authors:  Barbara Petschacher; Nicole Staunig; Monika Müller; Martin Schürmann; Daniel Mink; Stefaan De Wildeman; Karl Gruber; Anton Glieder
Journal:  Comput Struct Biotechnol J       Date:  2014-02-26       Impact factor: 7.271

  3 in total

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