Chávez S, Candau P
Departamento de Bioquimica Vegetal y Biologia Molecular, Universidad de Sevilla y CSIC, Spain.
FEBS Lett. 1991 Jul 8;285(1):35-8. doi: 10.1016/0014-5793(91)80719-j.
The unicellular cyanobacterium Synechocystis sp. PCC 6803 presents a hexameric NAD-specific glutamate dehydrogenase with a molecular mass of 295 kDa. The enzyme differs from the NADP-glutamate dehydrogenase found in the same strain and is coded by a different gene. NAD-glutamate dehydrogenase shows a high coenzyme specificity, catalyzes preferentially glutamate formation and presents Km values for ammonium, NADH and 2-oxoglutarate of 4.5 mM, 50 microM and 1.8 mM respectively. An animating role for the enzyme is discussed.
单细胞蓝藻聚球藻属6803菌株呈现出一种分子量为295 kDa的六聚体NAD特异性谷氨酸脱氢酶。该酶与同一菌株中发现的NADP-谷氨酸脱氢酶不同,由不同的基因编码。NAD-谷氨酸脱氢酶表现出高辅酶特异性,优先催化谷氨酸的形成,其对铵、NADH和2-氧代戊二酸的Km值分别为4.5 mM、50 μM和1.8 mM。文中讨论了该酶的激活作用。