A new D-stereospecific amino acid amidase from Ochrobactrum anthropi.
A new D-stereospecific amino acid amidase from Ochrobactrum anthropi.
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来自人苍白杆菌的新型 D-立体特异性氨基酸酰胺酶。
DOI：
10.1016/0006-291x(89)92021-4
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发表时间：
1989
影响因子：
3.1
通讯作者：
A. Nakazawa
中科院分区：
文献类型：
--
作者：
Y. Asano;Tsutomu Mori;S. Hanamoto;Y. Kato;A. Nakazawa
从土壤中分离和筛选的人类嗜铬杆菌（mochrobacum anthropiSCRC SV3）中部分纯化出一种新的d立体特异性氨基酸酰胺酶。该酶的mr估计约为38,000，其等电点为5.3。该酶催化d -氨基酸酰胺的立体特异性水解生成d -氨基酸和氨。主要底物包括d -苯丙氨酸酰胺、d -酪氨酸酰胺、d -色氨酸酰胺、d -亮氨酸酰胺和d -丙氨酸酰胺。
A new D-stereospecific amino acid amidase has been partially purified fromOchrobactrum anthropiSCRC SV3, which had been isolated and selected from soil. TheMrof the enzyme was estimated to be about 38,000, and its isoelectric point was 5.3. The enzyme catalyzes the stereospecific hydrolysis of D-amino acid amide to yield D-amino acid and ammonia. The major substrates included D-phenylalanine amide, D-tyrosine amide, D-tryptophan amide, D-leucine amide, and D-alanine amide.