角鲨M4乳酸脱氢酶：被磷酸吡哆醛可逆失活，并在模拟活性三元复合物的复合物中得到完全保护。
Dogfish M4 lactate dehydrogenase: reversible inactivation by pyridoxal 5'-phosphate and complete protection in complexes that mimic the active ternary complex.
作者信息
Chen S S, Engel P C
出版信息
Biochem J. 1975 Nov;151(2):447-9. doi: 10.1042/bj1510447.
Abstract
Dogfish M4 lactate dehydrogenase, like the corresponding pig enzyme, is inactivated by pyridoxal 5'-phosphate through modification of a single essential lysine residue. The activity is completely protected in the complexes E-NAD+-oxalate, E-NADH-oxamate and E-(NAD+-pyruvate adduct), but only partially protected in E-NAD+, E-NADH, E-NAD+-oxamate and E-NADH-oxalate.
摘要
角鲨M4乳酸脱氢酶与相应的猪酶一样，通过修饰单个必需赖氨酸残基被5'-磷酸吡哆醛灭活。在E-NAD+-草酸盐、E-NADH-草氨酸盐和E-（NAD+-丙酮酸加合物）复合物中活性得到完全保护，但在E-NAD+、E-NADH、E-NAD+-草氨酸盐和E-NADH-草酸盐中仅得到部分保护。
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The equilibrium position of the reaction of bovine liver glutamate dehydrogenase with pyridoxal5'-phosphate. A demonstration that covalent modification with this reagent completely abolishes catalytic activity.牛肝谷氨酸脱氢酶与磷酸吡哆醛反应的平衡位置。证明用该试剂进行共价修饰会完全消除催化活性。
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