Affenzeller K, Jaklitsch W M, Hönlinger C, Kubicek C P
Department of Microbial Biochemistry, Vienna Technical University, Austria.
FEMS Microbiol Lett. 1989 Apr;49(2-3):293-7. doi: 10.1016/0378-1097(89)90056-6.
A partially purified preparation of alpha-aminoadipate reductase (EC 1.2.1.31) from Penicillium chrysogenum is competitively inhibited by lysine (Ki of 0.26 mM). Exogenous addition of 10 mM L-lysine to resting mycelia of P. chrysogenum increased the intracellular lysine pool concentration 2-fold, but decreased the incorporation of (6-14C)-alpha-aminoadipate into protein-bound lysine to a fifth. The distribution of radioactivity in the pathway metabolites alpha-aminoadipate, saccharopine and lysine was consistent with the assumption of a lysine sensitive enzyme step in vivo between alpha-aminoadipate and saccharopine. Hence lysine inhibition of alpha-aminoadipate reductase may be of physiologic importance.
产黄青霉中部分纯化的α-氨基己二酸还原酶（EC 1.2.1.31）制剂受到赖氨酸的竞争性抑制（Ki为0.26 mM）。向产黄青霉静止菌丝体中外源添加10 mM L-赖氨酸可使细胞内赖氨酸池浓度增加2倍，但将(6-¹⁴C)-α-氨基己二酸掺入蛋白质结合赖氨酸的量降至五分之一。放射性在途径代谢物α-氨基己二酸、酵母氨酸和赖氨酸中的分布与体内α-氨基己二酸和酵母氨酸之间存在赖氨酸敏感酶步骤的假设一致。因此，赖氨酸对α-氨基己二酸还原酶的抑制可能具有生理重要性。
