Purification, properties and reactivity of the esterase from Micrococcus sp.
The esterase from Micrococcus sp., which hydrolyzes n-propyl-2-fluorocyclopropanecarboxylate (3) enantioselectively, was highly purified by three types of chromatography. The purified enzyme was inactivated by Hg and diisopropyl fluorophosphate (DFP). It was a monomer with a molecular weight of about 35000. The enzyme exhibits esterase activity towards many aliphatic propyl esters. The enantioselectivity for substrate (3) using purified enzyme did not differ from that of crude enzyme.
Imura
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Chemical Technology Research Laboratories, Daiichi Pharmaceutical Co., Ltd., Tokyo, Japan.
Itoh
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Miyadera
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D004950:Esterases / Q000302:isolation & purification* / Q000378:metabolism; D008837:Micrococcus / Q000201:enzymology*; D008970:Molecular Weight; D013379:Substrate Specificity
D004950:Esterases