Substrate selectivities of proline hydroxylases
Substrate selectivities of proline hydroxylases
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DOI：
10.1016/s0040-4039(99)00944-2
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发表时间：
1999-07-09
影响因子：
1.8
通讯作者：
Ozaki, A
中科院分区：
文献类型：
--
作者：
Shibasaki, T;Sakurai, W;Ozaki, A
研究了从重组大肠杆菌中纯化的微生物脯氨酸4-羟化酶和脯氨酸3-羟化酶的底物选择性。L-2-氮杂环丁烷羧酸酯、3，4-脱氢-L-脯氨酸和L-哌啶酸在这些酶的作用下发生了区域和立体专一性的羟基化反应。(C)1999爱思唯尔科技有限公司。保留所有权利。
Substrate selectivities of microbial proline 4-hydroxylase and proline 3-hydroxylases, all of which were purified from recombinant Escherichia coli, were investigated. L-2-Azetidine carboxylate, 3,4-dehydro-L-proline and L-pipecolinic acid were hydroxylated by those enzymes in regio- and stereospecific manner. (C) 1999 Elsevier Science Ltd. All rights reserved.