期刊
ADVANCED SYNTHESIS & CATALYSIS
卷 360, 期 2, 页码 242-249出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/adsc.201701282
关键词
Acyl transferase; Hydrolase; Kinetic resolution; Mycobacterium smegmatis; Transesterification; Water
资金
- University of Trieste
- region Friuli Venezia Giulia
- Austrian Science Fund (FWF) [J3292]
- Netherlands Organisation for Scientific Research (NWO) [14170]
- Austrian Science Fund (FWF) [J3292] Funding Source: Austrian Science Fund (FWF)
The acyl transferase from Mycobacterium smegmatis (MsAcT) catalyses transesterification reactions in aqueous media because of its hydrophobic active site. Aliphatic cyanohydrin and alkyne esters can be synthesised in water with excellent and strikingly opposite enantioselectivity [(R); E>37 and (S); E> 100, respectively]. When using this enzyme, the undesired hydrolysis of the acyl donor is an important factor to take into account. Finally, the choice of acyl donor can significantly influence the obtained enantiomeric excesses.
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