KINETIC RESOLUTION OF UNNATURAL AND RARELY OCCURRING AMINO-ACIDS - ENANTIOSELECTIVE HYDROLYSIS OF N-ACYL AMINO-ACIDS CATALYZED BY ACYLASE-I
KINETIC RESOLUTION OF UNNATURAL AND RARELY OCCURRING AMINO-ACIDS - ENANTIOSELECTIVE HYDROLYSIS OF N-ACYL AMINO-ACIDS CATALYZED BY ACYLASE-I
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DOI：
10.1021/ja00198a055
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发表时间：
1989-08-02
影响因子：
15
通讯作者：
WHITESIDES, GM
中科院分区：
文献类型：
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作者：
CHENAULT, HK;DAHMER, J;WHITESIDES, GM
酰基酶I(Ainoacylase；N-acyl氨基酸氨基水解酶，EC 3.5.1.14，来自猪肾和真菌曲霉)是一种广泛适用的酶催化剂，用于动力学拆分非天然和罕见的α-氨基酸。它对N-酰基L-α-氨基酸的对映体选择性几乎是绝对的，但它可以接受具有广泛结构的官能团的底物。本文报道了50多种N-酰基氨基酸及其类似物的酶催化初始水解率，酶在水和水/有机溶液中的稳定性，以及不同酰基和金属离子对酶水解率的影响。在2-29克尺度上拆分了11种α-氨基酸和α-甲基-α-氨基酸。粗L-和D-氨基酸产品一般含有90%的ee。通过(R)-和(S)-1-丁烯氧化物的制备和3个2-氨基-4-烯酸衍生物的非对映选择性(顺式：反式，7-8：1)碘内酯化反应，说明了可拆分氨基酸作为手性合成子的用途。
Acylase I (aminoacylase; N-acylamino-acid amidohydrolase, EC 3.5.1.14, from porcine kidney and the fungus Aspergillus) is a broadly applicable enzymatic catalyst for the kinetic resolution of unnatural and rarely occurring .alpha.-amino acids. Its enantioselectivity for the hydrolysis of N-acyl L-.alpha.-amino acids is nearly absolute, yet it accepts substrates having a wide range of structure of functionality. This paper reports the initial rates of enzyme-catalyzed hydrolysis of over 50 N-acyl amino acids and analogues, the stabilities of the enzymes in aqueous and aqueous/organic solutions, and the effects of different acyl groups and metal ions on the rates of enzymatic hydrolysis. Eleven .alpha.-amino and .alpha.-methyl .alpha.-amino acids were resolved on a 2-29-g scale. Crude L- and D-amino acid products had generally > 90% ee. The utility of resolved amino acids as chiral synthons was illustrated by the preparation of (R)- and (S)-1-butene oxide and the diastereoselective (cis:trans, 7-8:1) iodolactonization of three 2-amino-4-alkenoic acid derivatives.