The specificity and kinetic mechanism of branched-chain amino acid aminotransferase fromEscherichia colistudied with a new improved coupled assay procedure and the enzyme's potential for biocatalysis

Development of a satisfactory and general continuous assay for aminotransferases by coupling with (R)-2-hydroxyglutarate dehydrogenase

(2012) Xuejing Yu et al.   ANALYTICAL BIOCHEMISTRY

A robust methodology for kinetic model parameter estimation for biocatalytic reactions

(2012) Naweed Al-Haque et al.   BIOTECHNOLOGY PROGRESS

Transaminases for the synthesis of enantiopure beta-amino acids

(2012) Jens Rudat et al.   AMB Express

Enzymatic Synthesis of L-tert-Leucine with Branched Chain Aminotransferase

(2011) Young-Man Seo   JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY

Forced evolution ofEscherichia colicells with the ability to effectively utilize non-natural amino acidsl-tert-leucine,l-norleucine and γ-methyl-l-leucine

(2010) Xing-Guo Wang et al.   BIOCATALYSIS AND BIOTRANSFORMATION

Asymmetric synthesis of l-tert-leucine and l-3-hydroxyadamantylglycine using branched chain aminotransferase

(2010) Eun young Hong et al.   JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC