Metal substitution in thermolysin: Catalytic properties of tungstate thermolysin in sulfoxidation with H2O2
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The catalytic Zn2+ ion was extracted from thermolysin, which had been covalently bound to Eupergit C. The apo-enzyme incorporated the oxometallate anions MoO42, SeO42, and WO42 with partial restoration of the proteolytic activity. Tungstate thermolysin was moderately active in the sulfoxidation of thioanisole by hydrogen peroxide, whereas its activity towards phenylmercaptoacetophenone, which was designed to bind well in the active site of thermolysin, was much higher.
1979 ◽
Vol 44
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pp. 1015-1022
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1988 ◽
Vol 53
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pp. 1636-1646
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1984 ◽
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pp. 14-24
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1978 ◽
Vol 40
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pp. 1277-1278
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1999 ◽
Vol 362
(1)
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pp. 167-174
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1992 ◽
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pp. 507-519
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1996 ◽
Vol 111
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pp. 81-90
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