6-重氮-5-氧代-L-正亮氨酸和偶氮丝氨酸作为谷氨酰胺（天冬酰胺）酶的亲和抑制剂。
6-diazo-5-oxo-L-norleucine and azaserine as affinity inhibitors of glutamin(asparagin)ase.
作者信息
Lebedeva Z I, Kabanova E A, Berezov T T
出版信息
Biochem Int. 1986 Mar;12(3):413-20.
Incubation of homogeneous glutamin(asparagin)ase from Pseudomonas aurantiaca with 6-diazo-5-oxo-L-norleucine (DON) and azaserine leads to an almost complete inactivation of the enzyme. The inactivation process in both cases involves the step of reversible binding of the enzyme with the inhibitor into a complex and subsequent modification of the enzyme within this complex. The data on saturation of the enzyme by low concentrations of inhibitors, the protective effect of substrate and its analogs as well as of the competitive inhibitor and product of the enzymatic reaction, L-aspartate, suggest that the modification of functional groups takes place in the enzyme active site. The presence of essential threonine hydroxyl groups in/or near the enzyme active site is surmised.
用6-重氮-5-氧代-L-正亮氨酸（DON）和重氮丝氨酸孵育来自橙色假单胞菌的均一谷氨酰胺（天冬酰胺）酶会导致该酶几乎完全失活。在这两种情况下，失活过程都包括酶与抑制剂可逆结合形成复合物的步骤，以及随后在该复合物中对酶进行修饰。低浓度抑制剂对酶的饱和数据、底物及其类似物以及竞争性抑制剂和酶促反应产物L-天冬氨酸的保护作用表明，官能团的修饰发生在酶的活性位点。推测在酶活性位点内或附近存在必需的苏氨酸羟基。
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