Asymmetric reductive amination by a wild-type amine dehydrogenase from the thermophilic bacteria Petrotoga mobilis

BioChem - DOS

Search

메타 데이터

바이오화학분류

- 바이오정밀화학
  1. 기타
- 화장품용 기능성소재
  1. 기능성

논문

Asymmetric reductive amination by a wild-type amine dehydrogenase from the thermophilic bacteria Petrotoga mobilis

학술지

Catalysis science & technology

저자명

Mayol, Ombeline; David, Sylvain; Darii, Ekaterina; Debard, Adrien; Mariage, Aline; Pellouin, Virginie; Petit, Jean-Louis; Salanoubat, Marcel; de Berardinis, Vé ronique; Zaparucha, Anne; Vergne-Vaxelaire, Carine

초록

The biocatalytic reductive amination of ketone to chiral amine is one of the most challenging reactions. Using a genome-mining approach, we found proteins catalyzing the reductive amination of ketones without a carboxylic function in the α or β position. The synthesis of (4S)-4-aminopentanoic acid (ee ≥99.5%) was achieved with the thermoactive amine dehydrogenase (AmDH) AmDH4 fromPetrotoga mobilisin 88% yield. The high stability and substrate tolerance make AmDH4 a very good starting point for further discovery of reductive amination biocatalysts with an enlarged substrate range. This is the first report of wild-type enzymes with related genes having proper NAD(P)H-AmDH activity.

발행연도

2016

발행기관

The Royal Society of Chemistry

ISSN

2044-4753

ISSN

2044-4761

권

호

페이지

pp.7421-7428