Larsson O M, Schousboe A
Department of Biological Sciences, Royal Danish School of Pharmacy, Copenhagen.
Neurochem Res. 1990 Nov;15(11):1073-7. doi: 10.1007/BF01101706.
The enzymatic mechanism and the kinetic parameters of GABA-transaminase extracted from cultured mouse cerebral cortex neurons and astrocytes were studied. Neuronal as well as astrocytic GABA-transaminase obeyed a bi bi ping-pong reaction mechanism. The estimated Km-values for alpha-ketoglutarate and GABA were significantly lower for astroglial GABA-transaminase compared to the neuronal enzyme suggesting a possible existence of cell specific isozymes of GABA-transaminase. The observed enzymatic mechanism and the magnitude of the estimated kinetic parameters imply that GABA-transaminase synthesized in the two types of cultured neural cells is mechanistically and kinetically equivalent to the enzyme synthesized in the brain in vivo.
对从培养的小鼠大脑皮质神经元和星形胶质细胞中提取的γ-氨基丁酸转氨酶(GABA转氨酶)的酶促机制和动力学参数进行了研究。神经元型和星形胶质细胞型GABA转氨酶均遵循双底物双产物乒乓反应机制。与神经元酶相比,星形胶质细胞GABA转氨酶对α-酮戊二酸和GABA的估计Km值显著更低,这表明可能存在GABA转氨酶的细胞特异性同工酶。观察到的酶促机制和估计的动力学参数大小意味着在两种培养的神经细胞中合成的GABA转氨酶在机制和动力学上与体内大脑中合成的酶相当。