Enzymatic synthesis of L-tert-leucine with branched chain aminotransferase.
In this study, we demonstrated the asymmetric synthesis of L-tert-leucine from trimethylpyruvate using branchedchain 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.
School of Biotechnology, Yeungnam University, Gyeongsan, Gyeongbuk 712-749, Korea.
Young-Man
YM
Seo
Hyungdon
H
Yun
D001219:Aspartate Aminotransferases / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D018698:Glutamic Acid / Q000378:metabolism; D007930:Leucine / Q000096:biosynthesis*; D011767:Pyruvate Decarboxylase / Q000235:genetics / Q000378:metabolism; D000637:Transaminases / Q000235:genetics / Q000378:metabolism*
D029968:Escherichia coli Proteins; D018698:Glutamic Acid; D000637:Transaminases; D001219:Aspartate Aminotransferases; C019798:branched-chain-amino-acid transaminase; D011767:Pyruvate Decarboxylase; D007930:Leucine