Limonene-1,2-Epoxide Hydrolase fromRhodococcus erythropolis DCL14 Belongs to a Novel Class of Epoxide Hydrolases
Limonene-1,2-Epoxide Hydrolase fromRhodococcus erythropolis DCL14 Belongs to a Novel Class of Epoxide Hydrolases
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来自红平红球菌 DCL14 的柠檬烯-1,2-环氧化物水解酶属于一类新型环氧化物水解酶
DOI：
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发表时间：
1998
影响因子：
3.2
通讯作者：
J. D. de Bont
中科院分区：
文献类型：
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作者：
M. J. van der Werf;K. Overkamp;J. D. de Bont
ABSTRACT An epoxide hydrolase from Rhodococcus erythropolisDCL14 catalyzes the hydrolysis of limonene-1,2-epoxide to limonene-1,2-diol. The enzyme is induced when R. erythropolis is grown on monoterpenes, reflecting its role in the limonene degradation pathway of this microorganism. Limonene-1,2-epoxide hydrolase was purified to homogeneity. It is a monomeric cytoplasmic enzyme of 17 kDa, and its N-terminal amino acid sequence was determined. No cofactor was required for activity of this colorless enzyme. Maximal enzyme activity was measured at pH 7 and 50°C. None of the tested inhibitors or metal ions inhibited limonene-1,2-epoxide hydrolase activity. Limonene-1,2-epoxide hydrolase has a narrow substrate range. Of the compounds tested, only limonene-1,2-epoxide, 1-methylcyclohexene oxide, cyclohexene oxide, and indene oxide were substrates. This report shows that limonene-1,2-epoxide hydrolase belongs to a new class of epoxide hydrolases based on (i) its low molecular mass, (ii) the absence of any significant homology between the partial amino acid sequence of limonene-1,2-epoxide hydrolase and amino acid sequences of known epoxide hydrolases, (iii) its pH profile, and (iv) the inability of 2-bromo-4′-nitroacetophenone, diethylpyrocarbonate, 4-fluorochalcone oxide, and 1,10-phenanthroline to inhibit limonene-1,2-epoxide hydrolase activity.
DOI：
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发表时间：
1994-04
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
L. Orning;J. Gierse;F. Fitzpatrick
通讯作者：
L. Orning;J. Gierse;F. Fitzpatrick