Discovery of a novel ortho-haloacetophenones-specific carbonyl reductase from Bacillus aryabhattai and insight into the molecular basis for its catalytic performance

Aipeng Li, Qingxiao Yuchi, Xue Li, Wei Pang, Bin Li, Feng Xue, Lianbing Zhang

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

To exploit robust biocatalysts for chiral 1-(2-halophenyl)ethanols synthesis, an ortho-haloacetophenones-specific carbonyl reductase (BaSDR1) gene from Bacillus aryabhattai was cloned and expressed in Escherichia coli. The impressive properties regarding BaSDR1 application include preference for NADH as coenzyme, noticeable tolerance against high cosubstrate concentration, and remarkable catalytic performance over a broad pH range from 5.0 to 10.0. The optimal temperature was 35 °C, with a half-life of 3.1 h at 35 °C and 0.75 h at 45 °C, respectively. Notably, BaSDR1 displayed excellent catalytic performance toward various ortho-haloacetophenones, providing chiral 1-(2-halophenyl)ethanols with 99% ee for all the substrates tested. Most importantly, the docking results indicated that the enzyme-substrate interactions and the steric hindrance of halogen atoms act in a push-pull manner in regulating enzyme catalytic ability. These results provide valuable clues for the structure-function relationships of BaSDR1 and the role of halogen groups in catalytic performance, and offer important reference for protein engineering and mining of functional compounds.

Original languageEnglish
Pages (from-to)781-790
Number of pages10
JournalInternational Journal of Biological Macromolecules
Volume138
DOIs
StatePublished - 1 Oct 2019

Keywords

  • Asymmetric reduction
  • Carbonyl reductase
  • ortho-Haloacetophenones

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