Stereospecific labeling at α-position of phenylalanine and phenylglycine with amino acid racemase
Stereospecific labeling at α-position of phenylalanine and phenylglycine with amino acid racemase
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DOI：
10.1016/s0922-338x(99)89012-6
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发表时间：
1998-01-01
期刊：
影响因子：
--
通讯作者：
Esaki, N
中科院分区：
文献类型：
--
作者：
Lim, YH;Yoshimura, T;Esaki, N
从恶臭假单胞菌ATCC 17642纯化的具有低底物特异性的氨基酸消旋酶（EC 5.1.1.10）催化各种氨基酸的消旋化，但不催化芳香族和酸性氨基酸的消旋化。然而，苯丙氨酸和苯甘氨酸经历α-氢交换与氘从溶剂中培养时，消旋酶在氧化氘。α-氘代苯丙氨酸和苯基甘氨酸的每种对映体都是立体特异性地产生的，保留了C-2构型。该α-氢交换反应适用于α-氘代苯丙氨酸和苯甘氨酸的生产。
Amino acid racemase with low substrate specificity (EC 5.1.1.10) purified from Pseudomonas putida ATCC17642 catalyzes the racemization of various amino acids but not that of aromatic and acidic amino acids. However, phenylalanine and phenylglycine underwent alpha-hydrogen exchange with deuterium from the solvent when incubated with the racemase in deuterium oxide. Each enantiomer of both alpha-deuterated phenylalanine and phenylglycine was produced stereospecifically with retention of the C-2 configuration. This alpha-hydrogen exchange reaction is applicable to the production of alpha-deuterated phenylalanine and phenylglycine.