Azidolysis of epoxides catalysed by the halohydrin dehalogenase from Arthrobacter sp AD2 and a mutant with enhanced enantioselectivity: an (S)-selective HHDH

作者：Mikleusevic, Ana; Primozic, Ines; Hrenar, Tomica; Salopek-Sondi, Branka; Tang, Lixia; Elenkov, Maja Majeric^*

来源：Tetrahedron: Asymmetry , 2016, 27(19): 930-935.

DOI：10.1016/j.tetasy.2016.08.003

• SP STRAIN AD2
• HALOALCOHOL DEHALOGENASE
• KINETIC RESOLUTION
• 2,2-DISUBSTITUTED EPOXIDES
• AGROBACTERIUM-RADIOBACTER
• BIOCATALYTIC AZIDOLYSIS
• PURIFICATION
• LIGANDS
• DENSITY
• FAMILY

Halohydrin dehalogenase from Arthrobacter sp. AD2 catalysed azidolysis of epoxides with high regioselectivity and low to moderate (S)-enantioselectivity (E = 1-16). Mutation of the asparagine 178 to alanine (N178A) showed increased enantioselectivity towards styrene oxide derivatives and glycidyl ethers. Conversion of aromatic epoxides was catalysed by HheA-N178A with complete enantioselectivity, however the regioselectivity was reduced. As a result of the enzyme-catalysed reaction, enantiomerically pure (S)-beta-azido alcohols and (R)-alpha-azido alcohols (ee >= 99%) were obtained.

• 出版日期2016-10-15