Thermophilic alanine dehydrogenase from Halobacterium salinarium.
Thermophilic alanine dehydrogenase from Halobacterium salinarium.
复制标题
来自盐盐杆菌的嗜热丙氨酸脱氢酶。
DOI：
10.1139/o74-144
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发表时间：
1974
期刊：
影响因子：
--
通讯作者：
K. Wulff
中科院分区：
文献类型：
--
作者：
D. Keradjopoulos;K. Wulff
来自盐生盐杆菌的丙氨酸脱氢酶（L-丙氨酸：NAD+氧化还原酶（脱氨基），EC 1.4.1.1）需要高浓度的NaCl以获得活性和稳定性。该酶是嗜热的，在3.4 M KCl中的最适温度为70 °C，在3.4 M NaCl中的最适温度为60 °C。 另外六种酶也具有嗜热性。盐疗室。如果NaCl浓度降至1.5M以下，丙氨酸脱氢酶失活，如果盐浓度增加至4 M，丙氨酸脱氢酶重新活化。 两种反应，灭活和再活化，都需要2-巯基乙醇的存在才能完全再活化。再活化反应被N-乙基马来酰亚胺不可逆地抑制。
Alanine dehydrogenase (L-alanine:NAD+ oxidoreductase (deaminating), EC 1.4.1.1) from Halobacterium salinarium requires high concentrations of NaCl for both activity and stability. The enzyme is thermophilic with an optimum temperature of 70 °C in 3.4 M KCl and of 60 °C in 3.4 M NaCl. A thermophilic character has also been found for six other enzymes from H. salinarium. The alanine dehydrogenase becomes inactivated if the NaCl concentration drops below 1.5 M and it becomes reactivated if the salt concentration is increased to 4 M. Both reactions, the inactivation as well as the reactivation, require the presence of 2-mercaptoethanol for a complete reactivation. The reactivation reaction is irreversibly inhibited by N-ethylmaleimide.