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

Title
Enzymatic Synthesis of L-tert-Leucine with Branched Chain Aminotransferase
Author(s)
윤형돈서영만[서영만]
Keywords
PENICILLIN-G ACYLASE; ASYMMETRIC-SYNTHESIS; KINETIC RESOLUTION; ALPHA-AMINO; TRANSAMINASES; BIOCATALYSIS; ACIDS
Issue Date
201110
Publisher
KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
Citation
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.21, no.10, pp.1049 - 1052
Abstract
In this study, we demonstrated the asymmetric synthesis of L-tert-leucine from trimethylpyruvate using branched-chain aminotransferase (BCAT) from Escherichia coli in the presence of L-glutamate as an amino donor. Since BCAT was severely inhibited by 2-ketoglutarate, in order to overcome this here, we developed a BCAT/aspartate aminotransferase (AspAT) and BCAT/AspAT/pyruvate decarboxylase (PDC) coupling reaction. In the BCAT/AspAT/PDC coupling reaction, 89.2 mM L-tert-leucine (ee >99%) was asymmetrically synthesized from 100 mM trimethylpyruvate.
URI
http://hdl.handle.net/YU.REPOSITORY/24411http://dx.doi.org/10.4014/jmb.1105.05049
ISSN
1017-7825
Appears in Collections:
생명공학부 > 생명공학부 > Articles
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE