Miflin B J, Lea P J
Biochem J. 1975 Aug;149(2):403-9. doi: 10.1042/bj1490403.
Glutamine, in the presence of alpha-oxoglutarate, stimulates nicotinamide nucleotide oxidation by crude extracts of pea roots and leads to a reductant-dependent formation of glutamate. Commercially available asparagine also stimulates nicotinamide nucleotide oxidation in the presence of alpha-oxoglutarate, but the reaction causing the stimulation can occur in the absence of a reductant, is inhibited by transaminase inhibitors, and is additive to the glutamine reaction. The asparagine used was found to be contaminated with aspartate. Repurified asparagine, chromatographically free of aspartate, did not stimulate the rate of nicotinamide nucleotide oxidation, and it is probable that the original stimulation was due to aspartate contamination. It is concluded that pea-root glutamine (amide)-alpha-oxoglutarate aminotransferase (glutamate synthase), in common with the enzyme in leaves, is specific for glutamine as the N donor and alpha-oxoglutarate as the N acceptor. The significance of the enzyme in conjunction with glutamine synthetase in the assimilation of nitrate by roots is discussed.
在α-酮戊二酸存在的情况下,谷氨酰胺可刺激豌豆根粗提物对烟酰胺核苷酸的氧化,并导致依赖还原剂的谷氨酸形成。市售的天冬酰胺在α-酮戊二酸存在时也能刺激烟酰胺核苷酸的氧化,但引起刺激的反应可在无还原剂的情况下发生,会受到转氨酶抑制剂的抑制,且与谷氨酰胺反应具有加和性。所用的天冬酰胺被发现被天冬氨酸污染。经色谱法纯化且不含天冬氨酸的天冬酰胺不会刺激烟酰胺核苷酸的氧化速率,最初的刺激可能是由于天冬氨酸污染所致。得出的结论是,豌豆根谷氨酰胺(酰胺)-α-酮戊二酸转氨酶(谷氨酸合酶)与叶片中的酶一样,对谷氨酰胺作为氮供体和α-酮戊二酸作为氮受体具有特异性。讨论了该酶与谷氨酰胺合成酶共同作用在根对硝酸盐同化中的意义。