在中度嗜盐细菌中表达的人脑丝氨酸消旋酶的纯化与鉴定
Purification and characterization of human brain serine racemase expressed in moderately halophilic bacteria.
作者信息
Nagayoshi Chizuru, Ishibashi Matsujiro, Tokunaga Masao
机构信息
Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan.
出版信息
Protein Pept Lett. 2009;16(2):201-6. doi: 10.2174/092986609787316261.
We have successfully expressed an active human brain serine racemase (hSR) with His-tag using moderate halophile. The purified His-hSR showed high elimination and racemization activities on L-serine: the elimination activity was 2.6-fold higher than racemization activity. Both enzyme activities showed an optimum reaction pH at around 9.0 and were stimulated 5- to 7-fold by such divalent cations as Mg++, Mn++ and Ca++.
我们已成功利用嗜盐菌表达了带有His标签的活性人脑丝氨酸消旋酶（hSR）。纯化后的His-hSR对L-丝氨酸表现出较高的消除和消旋活性：消除活性比消旋活性高2.6倍。两种酶活性在pH约为9.0时均显示出最佳反应pH，并且受到Mg++、Mn++和Ca++等二价阳离子的5至7倍刺激。
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