ω-Transaminase-catalyzed kinetic resolution of chiral amines using l-threonine as an amino acceptor precursor

M. Shaheer Malik, Eul Soo Park, Jong Shik Shin

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

Kinetic resolution of chiral amines using l-threonine as a cosubstrate was demonstrated by a biocatalytic strategy in which (S)-selective ω-transaminase (ω-TA) was coupled with threonine deaminase (TD), eliminating the need to use an expensive keto acid as an amino acceptor. The coupled enzyme reaction enabled simultaneous production of enantiopure (R)-amine and l-homoalanine which are pharmaceutically important building blocks. To extend the versatility of this strategy to production of both enantiomers of chiral amines, (R)-selective ω-TA coupled with TD was employed to produce (S)-amine.

Original languageEnglish
Pages (from-to)2137-2140
Number of pages4
JournalGreen Chemistry
Volume14
Issue number8
DOIs
Publication statusPublished - 2012 Aug 1

Fingerprint

Threonine
Transaminases
Amines
Threonine Dehydratase
kinetics
Kinetics
Keto Acids
Enantiomers
Enzymes
enzyme
Acids
amine
acid

All Science Journal Classification (ASJC) codes

  • Environmental Chemistry
  • Pollution

Cite this

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ω-Transaminase-catalyzed kinetic resolution of chiral amines using l-threonine as an amino acceptor precursor. / Malik, M. Shaheer; Park, Eul Soo; Shin, Jong Shik.

In: Green Chemistry, Vol. 14, No. 8, 01.08.2012, p. 2137-2140.

Research output: Contribution to journalArticle

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