Talbot J C, Gros C, Cosson M P, Pantaloni D
Biochim Biophys Acta. 1977 Sep 27;494(1):19-32. doi: 10.1016/0005-2795(77)90131-3.
Kinetic studies of pyridoxal 5'-phosphate binding to glutamate dehydrogenase (EC 1.4.1.3) has provided evidence for two specific binding sites, chemically identified as Lys 126 and Lys 333. Use of protecting ligands permitted the selective modification of only one of these lysines, and showed that (1) Lys 333 modification results in depolymerisation of the enzyme into active hexamers; (2) Lys 126-modified enzyme was 92% inactivated. The residual activity was desensitized to GTP. The inactivation process was cooperative, maximum inactivation occurring as soon as half of the Lys 126 were modified.
对磷酸吡哆醛与谷氨酸脱氢酶（EC 1.4.1.3）结合的动力学研究为两个特定结合位点提供了证据，经化学鉴定为赖氨酸126和赖氨酸333。使用保护配体仅允许对其中一个赖氨酸进行选择性修饰，并表明：（1）赖氨酸333修饰导致酶解聚成活性六聚体；（2）赖氨酸126修饰的酶失活92%。残余活性对GTP不敏感。失活过程具有协同性，一旦一半的赖氨酸126被修饰，最大失活就会发生。
