Enzymatic activity and partial purification of solanapyrone synthase: first enzyme catalyzing Diels-Alder reaction
Enzymatic activity and partial purification of solanapyrone synthase: first enzyme catalyzing Diels-Alder reaction
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DOI：
10.1016/s0167-4838(98)00040-5
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发表时间：
1998-05-19
期刊：
影响因子：
--
通讯作者：
Ichihara, A
中科院分区：
文献类型：
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作者：
Katayama, K;Kobayashi, T;Ichihara, A
在茄链格孢菌（Alternaria solani）的细胞提取物中，发现了一种酶活性，通过氧化和随后的Diels-Alder反应将prosolanapyrone II转化为茄吡喃酮A和D。前一级分以2.2：1的比例将丙茄吡喃酮II转化为茄吡喃酮A和D，光学纯度分别为99%和45%ee。后一级分分别以7.6：1的比率以99%和接近0%ee这样做。从库2部分纯化的酶的天然分子量为40-62 kD，pi为4.25。丙茄吡喃酮III在水溶液中的高反应性和池2中酶的色谱行为表明，单一酶催化氧化和Diels-Alder反应。(C)1998 Elsevier Science B. V.保留所有权利。
In cell-foe extracts of Alternaria solani, an enzymatic activity converting prosolanapyrone II to solanapyrones A and D via oxidation and subsequent Diels-Alder reaction has been found. Chromatography with DEAE-Sepharose provided two active fractions, pools 1 and 2. The former fraction converted prosolanapyrone II to solanapyrones A and D in a ratio of 2.2:1 with optical purities of 99% and 45% ee, respectively. The latter fraction did so in a ratio of 7.6:1 with 99% and nearly 0% ee, respectively. The enzyme partially purified from pool 2 native molecular weight of 40-62 kD and a pi of 4.25. The high reactivity of prosolanapyrone III in aqueous solution and the chromatographic behavior of the enzyme in pool 2 suggest that a single enzyme catalyzes both the oxidation and Diels-Alder reaction. (C) 1998 Elsevier Science B.V. All rights reserved.